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Information on EC 1.9.6.1 - nitrate reductase (cytochrome)
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1.9.6.1 nitrate reductase (cytochrome)Specify your search results
Word Map
- 1.9.6.1
- nitrite
-
denitrification
-
denitrify
- molybdenum
- paracoccus
-
dissimilatory
- denitrificans
- n2o
- pantotrophus
- napf
-
nitrate-reducing
- desulfuricans
-
molybdoenzymes
-
thiosphaera
-
cyma
- fixk2
- menaquinol
-
di-haem
-
bismolybdopterin
-
wolinella
-
high-g
- narghi
-
norcbqd
-
nitrate-dependent
-
mo-containing
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
periplasmic nitrate reductase, periplasmic nitrate reductases, napedabc, napabc, nap-alpha, nap-beta, nap enzyme, benzyl viologen-nitrate reductase, napdaghb, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
benzyl viologen-nitrate reductase
-
-
-
-
EC 1.7.99.4
-
-
formerly, part transferred
-
mmol_1648
NAP
Nap-alpha
NAP-beta
NapA
NapAB
NapABC
NapDAGHB
NapEDABC
nitrate reductase, periplasmic
periplasmic nitrate reductase
periplasmic nitrate reductases
reductase, nitrate (cytochrome)
-
-
-
-
respiratory nitrate reductase
-
-
-
-
single subunit Nap-type periplasmic nitrate reductase
additional information
-
the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
-
-
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism. The second sphere type of mechanism is supported by the recent X-ray structures of Nap from Desulfovibrio desulf uricans ATCC 27774 and Cupriavidus necator H16, in which the sixth sulfur ligand of the Mo interacts with the sulfur from the cysteine residue and generates a bidentate persulfido ligand that sterically blocks the access of the substrate to the Mo ion, modelling
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome:nitrate oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY
9029-42-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrate + reduced acceptor
nitrite + oxidized acceptor
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
-
-
-
-
?
nitrite + methyl viologen
nitrate + oxidized methyl viologen
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
Cereibacter sphaeroides DSM 158
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 reduced methyl viologen + 2 H+ + nitrate
2 oxidized methyl viologen + nitrite
artificial electron acceptor
-
-
r
2 reduced methyl viologen + 2 H+ + nitrate
2 oxidized methyl viologen + nitrite
artificial electron acceptor
-
-
r
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the periplasmic cytochrome c-linked nitrate reductase is encoded by the napFDAGHBC operon. The napF operon apparently encodes a low-substrate-induced reductase that is maximally expressed only at low levels of nitrate. Expression is suppressed under high-nitrate conditions. In contrast, the narGHJI operon is only weakly expressed at low nitrate levels but is maximally expressed when nitrate is elevated. The narGHJI operon is therefore a high-substrate-induced operon that somehow provides a second and distinct role in nitrate metabolism by the cell. Nitrite, the end product of each enzyme, has only a minor effect on the expression of either operon. Finally, nitrate, but not nitrite, is essential for repression of napF gene expression. These studies reveal that nitrate rather than nitrite is the primary signal that controls the expression of these two nitrate reductase operons in a differential and complementary fashion
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
periplasmic nitrate reductase is expressed under nitrate-limiting conditions. NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinoneubiquinol couple via cytochrome NapC and NapB to NapA
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
Shewanella oneidensis MR-1 / ATCC 700550
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
electron transport chain in vivo: Fe3 + via specific cytochrome-nitrate reductase to NO3-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
very high substrate specificity. The enzyme does not reduce any other oxocompound (chlorate, bromate, iodate, nitrite, molybdate, sulphate, thiosulphate, tetrathionate, selenate, dimethyl sulphoxide, trimethylamine-A-oxide, borate and arsenate)
-
-
?
additional information
?
-
-
the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
-
-
?
additional information
?
-
-
the nap operon encodes the only nitrate reductase in Campylobacter jejuni and that it is essential in mediating growth using nitrate as a terminal electron acceptor under oxygen-limited conditions
-
-
?
additional information
?
-
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
-
-
?
additional information
?
-
Cereibacter sphaeroides DSM 158
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
-
-
?
additional information
?
-
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
-
NapABC enzyme is responsible for nitrate dissimilation. Periplasmic nitrate reductase (NapABC enzyme) can function in anaerobic respiration but does not constitute a site for generating proton motive force. napF-lacZ is expressed preferentially at relatively low nitrate concentrations in continuous cultures. This finding support the hypothesis that NapABC enzyme may function in Escherichia coli when low nitrate concentrations limit the bioenergetic efficiency of nitrate respiration via NarGHI enzyme
-
-
?
additional information
?
-
-
NapAB catalysed nitrate reduction driven by direct electron transfer from the electrode to NapAB, protein film voltammetry. Exploration of the nitrate reductase activity of purified NapAB as a function of electrochemical potential, substrate concentration and pH using protein film voltammetry. Nitrate reduction by NapAB occurs at potentials below approx. 0.1 V at pH 7. These are lower potentials than required for NarGH nitrate reduction. The potentials required for Nap nitrate reduction are also likely to require ubiquinol/ubiquinone ratios higher than are needed to activate the H+-pumping oxidases expressed during aerobic growth where Nap levels are maximal. Thus the operational potentials of Paracoccus pantotrophus NapAB are consistent with a productive role in redox balancing
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
Cereibacter sphaeroides DSM 158
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the periplasmic cytochrome c-linked nitrate reductase is encoded by the napFDAGHBC operon. The napF operon apparently encodes a low-substrate-induced reductase that is maximally expressed only at low levels of nitrate. Expression is suppressed under high-nitrate conditions. In contrast, the narGHJI operon is only weakly expressed at low nitrate levels but is maximally expressed when nitrate is elevated. The narGHJI operon is therefore a high-substrate-induced operon that somehow provides a second and distinct role in nitrate metabolism by the cell. Nitrite, the end product of each enzyme, has only a minor effect on the expression of either operon. Finally, nitrate, but not nitrite, is essential for repression of napF gene expression. These studies reveal that nitrate rather than nitrite is the primary signal that controls the expression of these two nitrate reductase operons in a differential and complementary fashion
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
periplasmic nitrate reductase is expressed under nitrate-limiting conditions. NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
electron transport chain in vivo: Fe3 + via specific cytochrome-nitrate reductase to NO3-
-
-
?
additional information
?
-
-
the nap operon encodes the only nitrate reductase in Campylobacter jejuni and that it is essential in mediating growth using nitrate as a terminal electron acceptor under oxygen-limited conditions
-
-
?
additional information
?
-
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
-
NapABC enzyme is responsible for nitrate dissimilation. Periplasmic nitrate reductase (NapABC enzyme) can function in anaerobic respiration but does not constitute a site for generating proton motive force. napF-lacZ is expressed preferentially at relatively low nitrate concentrations in continuous cultures. This finding support the hypothesis that NapABC enzyme may function in Escherichia coli when low nitrate concentrations limit the bioenergetic efficiency of nitrate respiration via NarGHI enzyme
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c552
-
the enzyme is a complex of a 93000 Da polypeptide and a 16000 Da nitrate-oxidizable cytochrome c552, cytochrome c552 contains two c-type heme moieties
-
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
subunit NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster
cytochrome
-
NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA
-
cytochrome
-
the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB
-
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
heme
-
contains 1.3 mol heme per mol of protein (assuminga 110-kDa molecular mass)
heme
-
the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB)
heme
O88111; O88160
a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor
molybdenum cofactor
i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
[4Fe-4S]-center
O88111; O88160
a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe2+
Iron
Mo
Mo(VI)
Mo5+
-
NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor. The molybdenum ion coordination sphere of NapA includes two molybdopterin guanine dinucleotide dithiolenes, a protein-derived cysteinyl ligand and an oxygen atom. The Mo-O bond length is 2.6 A, which is indicative of a water ligand. In NapA or NapAB, the Mo5+ state can not be further reduced to Mo4+. A catalytic cycle for NapA is proposed in which nitrate binds to the Mo5+ ion and where a stable des-oxo Mo6+ species may participate
Mo6+
-
NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor. The molybdenum ion coordination sphere of NapA includes two molybdopterin guanine dinucleotide dithiolenes, a protein-derived cysteinyl ligand and an oxygen atom. The Mo-O bond length is 2.6 A, which is indicative of a water ligand. In NapA or NapAB, the Mo5+ state can not be further reduced to Mo4+. A catalytic cycle for NapA is proposed in which nitrate binds to the Mo5+ ion and where a stable des-oxo Mo6+ species may participate
Molybdenum
Fe
-
subunit NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster
Fe
-
contains 2.7 mol iron (of which 1.4 mol is presumably non-haem iron) per mol of protein (assuming a 110000 Da molecular mass)
Iron
Fe:Mo ratio is slightly higher than the theoretical value of 4:1
Mo
-
subunit NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster
Mo
-
contains molybdenum, 0.9 mol molybdenum: 1 mol protein (assuminga 110000 Da molecular mass)
Mo(VI)
coordinates a cysteine and a sulfido residue
Molybdenum
92% Mo incorporation in active CNapA. The Fe:Mo ratio is slightly higher than the theoretical value of 4:1
Molybdenum
within the molybdenum cofactor. The coordination sphere of the Mo ion consists of the four thiolate ligands of two pyranopterins, a sulfur atom from a cysteine that attaches the MoCo to the protein backbone, and a sixth inorganic ligand, proposed to be oxygen or more recently sulfur
Molybdenum
O88111; O88160
the active site is a Mo bis-(pyranopterin guanine dinucleotide), relative metal content is around 1 Mo atom to 6 Fe atoms
Molybdenum
-
molybdenum-containing enzyme, the nitrate molecule binds to the active site with the molabdenum ion in the +6 oxidation state, electron transfer to the active site occurs only in the proton-electron transfer stage, where the molybdenum-V species plays an important role in catalysis
Molybdenum
in the molybdenum cofactor. Role for NapD in the insertion of the molybdenum cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nitrate
at high substrate concentration, substrate inhibition occurs, mechanism of substrate inhibition in Nap, and kinetics, overview
p-chloromercuribenzoate
-
0.3 mM, completely inhibits, can be reversed by cysteine or glutathione
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NapD
a small (9.3 kDa) cytoplasmic protein that is essential for Nap activity, role for NapD in the insertion of the molybdenum cofactor. The NapD cysteine residues (C8 and C32) are not conserved and a cysteine-free variant of NapD complements a DELTAnapD strain for restoration of NapA activity. A NapD C8S/C32A variant remains attached to the NapA signal peptide. Copurification of recombinant NapA complexed with N-terminally His-tagged NapD activator by nickel afinity chromatography
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
nitrate
-
pH 7, NapAB catalysed nitrate reduction driven by direct electron transfer from the electrode to NapAB, protein film voltammetry
additional information
additional information
steady-state kinetics during activation and inactivation of the enzyme, chronoamperometry, overview. The inactive species exists under three redox states, and the active form must exist in different redox states within the catalytic cycle
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
-
pH 7.0: about 70% of maximal activity, pH 9.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O88111 i.e. catalytic subunit NapA, O88160 i.e. electron transfer subunit NapB
O88111; O88160
UniProt
the genes for the periplasmic nitrate reductase are not part of the bacterial chromosome, but are located on the megaplasmid pHG1 present in the wild-type strain H16
-
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
mutant strain (M-6) overproduces the enzyme activity under anaerobic growth conditions
-
specific activity of the enzyme is higher in intact cells grown with butyrate than succinate as the sole source of carbon
-
specific activity of the enzyme is higher in intact cells grown with butyrate than succinate as the sole source of carbon
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
NapA is exported to the periplasm in a folded form by the twin-arginine protein transport (Tat) pathway. NapA is subject to Tat proofreading prior to export by the Tat pathway
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
genotyping of different strains from M and G populations, overview. The only mutated gene shared between the strains from populations M and G is bll4572, this gene is mutated in all six strains
evolution
periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans and formate dehydrogenase (Fdh) from Escherichia coli K-12, both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans belongs to the DMSO reductase family, subfamily I. Classification of Mo-pyranopterin dependent enzymes from the DMSO reductase family, e.g. periplasmic nitrate reductase and formate dehydrogenase, overview. Comparison of the sulfur-shift mechanism in nitrate reductase (Nap) and in formate dehydrogenase (Fdh), detailed overview
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans and formate dehydrogenase (Fdh) from Escherichia coli K-12, both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
Bradyrhizobium japonicum JCM 10833
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genotyping of different strains from M and G populations, overview. The only mutated gene shared between the strains from populations M and G is bll4572, this gene is mutated in all six strains
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evolution
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
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evolution
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
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evolution
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
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evolution
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
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malfunction
a gene nap deletion mutant can no longer grow on methanol in contrast to the wild-type and shows almost abolished N2O production from nitrate
malfunction
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Salmonella enterica serovar Typhimurium strains with defects in either nitrate reductase A (narG mutant) or the regulator inducing its transcription in the presence of high concentrations of nitrate (narL mutant) exhibit growth comparable to that of wild-type Salmonella enterica serovar Typhimurium. In contrast, a strain lacking a functional periplasmic nitrate reductase (napA mutant) exhibits a marked growth defect in the lumen of the colon. Inactivation of narP, encoding a response regulator that activates napABC transcription in response to low nitrate concentrations, significantly reduces the growth of Salmonella enterica serovar Typhimurium in the murine host gut lumen
malfunction
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Salmonella enterica serovar Typhimurium strains with defects in either nitrate reductase A (narG mutant) or the regulator inducing its transcription in the presence of high concentrations of nitrate (narL mutant) exhibit growth comparable to that of wild-type Salmonella enterica serovar Typhimurium. In contrast, a strain lacking a functional periplasmic nitrate reductase (napA mutant) exhibits a marked growth defect in the lumen of the colon. Inactivation of narP, encoding a response regulator that activates napABC transcription in response to low nitrate concentrations, significantly reduces the growth of Salmonella enterica serovar Typhimurium in the murine host gut lumen
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malfunction
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a gene nap deletion mutant can no longer grow on methanol in contrast to the wild-type and shows almost abolished N2O production from nitrate
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metabolism
cytochromes c encoded by genes in close proximity to the genes for XoxF proteins and methylamine dehydrogenase functions are likely involved in the metabolism with Nap, pathway overview
metabolism
NasST regulates the nitrate-mediated response of nosZ and napE genes, from the dissimilatory denitrification pathway, regulation of nos and nap genes by the NasST system in the absence of nitrate in mutant strains, overview
metabolism
Bradyrhizobium japonicum JCM 10833
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NasST regulates the nitrate-mediated response of nosZ and napE genes, from the dissimilatory denitrification pathway, regulation of nos and nap genes by the NasST system in the absence of nitrate in mutant strains, overview
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metabolism
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cytochromes c encoded by genes in close proximity to the genes for XoxF proteins and methylamine dehydrogenase functions are likely involved in the metabolism with Nap, pathway overview
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physiological function
the Nap-deficient mutant KD102 shows increased diauxic lag when switched from aerobic to anoxic respiration, suggesting Nap is responsible for shorter lags and helps in adaptation to anoxic metabolism after transition from aerobic conditions
physiological function
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napAB expression is required for anaerobic growth recovery by DELTAnarXL (a deletion encompassing the bulk of narXL)
physiological function
Escherichia coli is a Gram-negative bacterium that can use nitrate during anaerobic respiration. The catalytic subunit of the involved periplasmic nitrate reductase NapA contains two types of redox cofactor and is exported across the cytoplasmic membrane by the twin-arginine protein transport pathway
physiological function
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Salmonella enterica serovar Typhimurium uses the periplasmic nitrate reductase to support its growth on the low nitrate concentrations encountered in the gut, a strategy that may be shared with other enteric pathogens
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the single subunit nitrate reductase (Nap) appears to be involved in both the assimilatory and the dissimilatory denitrification pathways. The role in the former is supported by the methanol growth deficiency of the mutant when nitrate is used as a nitrogen source, and the role in the latter is supported by the lack of accumulation of N2O in the mutant
physiological function
a mutant strain defective for napA is not able to denitrify and grow on nitrate. The wild-type strain reaches 40 000 ppm of N2O emission and its growth is 10fold higher than that of the mutant strain. In the presence of nitrite as terminal electron acceptor, both wild-type and mutant are able to denitrify and to grow with no significant difference between both strains. NapA plays a role in Agrobacterium fabrum C58 fitness but is not involved in A. fabrum C58 root colonization
physiological function
the anaerobic reduction of NO3- to N2O is lower in Bradyrhizobium japonicum than in Bradyrhizobium diazoefficiens due to impaired periplasmic nitrate reductase (Nap) activity in B. japonicum. Impaired Nap activity in B. japonicum is due to low Nap protein levels
physiological function
the anaerobic reduction of NO3- to N2O is lower in Bradyrhizobium japonicum than in Bradyrhizobium diazoefficiens due to impaired periplasmic nitrate reductase (Nap) activity in B. japonicum. Impaired Nap activity in B. japonicum is due to low Nap protein levels
physiological function
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the anaerobic reduction of NO3- to N2O is lower in Bradyrhizobium japonicum than in Bradyrhizobium diazoefficiens due to impaired periplasmic nitrate reductase (Nap) activity in B. japonicum. Impaired Nap activity in B. japonicum is due to low Nap protein levels
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physiological function
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a mutant strain defective for napA is not able to denitrify and grow on nitrate. The wild-type strain reaches 40 000 ppm of N2O emission and its growth is 10fold higher than that of the mutant strain. In the presence of nitrite as terminal electron acceptor, both wild-type and mutant are able to denitrify and to grow with no significant difference between both strains. NapA plays a role in Agrobacterium fabrum C58 fitness but is not involved in A. fabrum C58 root colonization
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physiological function
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
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physiological function
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Salmonella enterica serovar Typhimurium uses the periplasmic nitrate reductase to support its growth on the low nitrate concentrations encountered in the gut, a strategy that may be shared with other enteric pathogens
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physiological function
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the single subunit nitrate reductase (Nap) appears to be involved in both the assimilatory and the dissimilatory denitrification pathways. The role in the former is supported by the methanol growth deficiency of the mutant when nitrate is used as a nitrogen source, and the role in the latter is supported by the lack of accumulation of N2O in the mutant
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physiological function
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the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
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additional information
modeling of regulation of nap and nos genes by NasST system in Bradyrhizobium japonicum strain USDA110 and nasS and Nos++ mutant strains
additional information
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modeling of regulation of nap and nos genes by NasST system in Bradyrhizobium japonicum strain USDA110 and nasS and Nos++ mutant strains
additional information
NapD is a small cytoplasmic protein that is essential for the activity of the periplasmic nitrate reductase and binds tightly to the twinarginine signal peptide of NapA. NapA is structured in its unbound form. The NapA signal peptide undergoes conformational rearrangement upon interaction with NapD. NapA is at least partially folded when bound by its NapD partner. The NapD chaperone binds primarily at the NapA signal peptide in this system and points towards a role for NapD in the insertion of the molybdenum cofactor
additional information
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NapD is a small cytoplasmic protein that is essential for the activity of the periplasmic nitrate reductase and binds tightly to the twinarginine signal peptide of NapA. NapA is structured in its unbound form. The NapA signal peptide undergoes conformational rearrangement upon interaction with NapD. NapA is at least partially folded when bound by its NapD partner. The NapD chaperone binds primarily at the NapA signal peptide in this system and points towards a role for NapD in the insertion of the molybdenum cofactor
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure, structure overview. Above the region of the metal center, the enzyme presents an arginine residue, Arg354,that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, Arg354,that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA, product of the napA gene, is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bis-PGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Paracoccus pantotrophus catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. But the Nap from Pseudomonas sp. G-179 lacks these two genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
additional information
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the Salmonella enterica serovar Typhimurium genome contains three nitrate reductases, encoded by the narGHI, narZYV, and napABC genes
additional information
Bradyrhizobium japonicum JCM 10833
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modeling of regulation of nap and nos genes by NasST system in Bradyrhizobium japonicum strain USDA110 and nasS and Nos++ mutant strains
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additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
-
additional information
-
the Salmonella enterica serovar Typhimurium genome contains three nitrate reductases, encoded by the narGHI, narZYV, and napABC genes
-
additional information
-
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. But the Nap from Pseudomonas sp. G-179 lacks these two genes
-
additional information
-
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bis-PGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Paracoccus pantotrophus catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NAPA1_PHOPR
Photobacterium profundum (strain SS9)
828
1
93366
Swiss-Prot
-
NAPA2_PHOPR
Photobacterium profundum (strain SS9)
830
0
92868
Swiss-Prot
-
NAPA_ACTP2
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
827
0
93572
Swiss-Prot
-
NAPA_ACTP7
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
827
0
93572
Swiss-Prot
-
NAPA_VIBCH
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
829
0
93106
Swiss-Prot
-
NAPA_VIBCM
Vibrio cholerae serotype O1 (strain M66-2)
829
0
93106
Swiss-Prot
-
NAPA_VIBPA
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
829
0
92961
Swiss-Prot
-
NAPA_WOLSU
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)
928
0
104968
Swiss-Prot
-
NAPA_YERE8
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
831
0
93407
Swiss-Prot
-
NAPA_YERP3
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
830
0
93256
Swiss-Prot
-
NAPA_YERPA
Yersinia pestis bv. Antiqua (strain Antiqua)
830
0
93226
Swiss-Prot
-
NAPA_YERPB
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
830
0
93256
Swiss-Prot
-
NAPA_YERPG
Yersinia pestis bv. Antiqua (strain Angola)
830
0
93256
Swiss-Prot
-
NAPA_YERPN
Yersinia pestis bv. Antiqua (strain Nepal516)
830
0
93226
Swiss-Prot
-
NAPA_YERPP
Yersinia pestis (strain Pestoides F)
830
0
93256
Swiss-Prot
-
NAPA_YERPS
Yersinia pseudotuberculosis serotype I (strain IP32953)
830
0
93256
Swiss-Prot
-
NAPA_YERPY
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
830
0
93256
Swiss-Prot
-
NAPA_HAEIE
Haemophilus influenzae (strain PittEE)
827
0
93713
Swiss-Prot
-
NAPA_HAHCH
Hahella chejuensis (strain KCTC 2396)
830
0
93708
Swiss-Prot
-
NAPA_HELHP
Helicobacter hepaticus (strain ATCC 51449 / 3B1)
937
0
105424
Swiss-Prot
-
NAPA_LARHH
Laribacter hongkongensis (strain HLHK9)
839
0
94304
Swiss-Prot
-
NAPA_LEPCP
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6)
851
0
94789
Swiss-Prot
-
NAPA_MAGSA
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
827
0
92939
Swiss-Prot
-
NAPA_MANSM
Mannheimia succiniciproducens (strain MBEL55E)
830
0
93765
Swiss-Prot
-
NAPA_NAUPA
Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH)
937
0
106622
Swiss-Prot
-
NAPA_PARXL
Paraburkholderia xenovorans (strain LB400)
827
0
92597
Swiss-Prot
-
NAPA_PECAS
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
828
0
92780
Swiss-Prot
-
NAPA_PECCP
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
828
0
92674
Swiss-Prot
-
NAPA_ACTPJ
Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
827
0
93572
Swiss-Prot
-
NAPA_ACTSZ
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z)
826
0
93338
Swiss-Prot
-
NAPA_AERHH
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049)
829
0
92843
Swiss-Prot
-
NAPA_AGGAC
828
0
93492
Swiss-Prot
-
NAPA_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
834
0
93527
Swiss-Prot
-
NAPA_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
829
0
92594
Swiss-Prot
-
NAPA_BORBR
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
829
0
92970
Swiss-Prot
-
NAPA_BORPA
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
831
0
93168
Swiss-Prot
-
NAPA_BORPD
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
847
0
94698
Swiss-Prot
-
NAPA_BRADU
Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
837
0
94215
Swiss-Prot
-
NAPA_BRASB
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
834
0
93602
Swiss-Prot
-
NAPA_CAMC1
Campylobacter concisus (strain 13826)
926
0
104218
Swiss-Prot
-
NAPA_CAMC5
Campylobacter curvus (strain 525.92)
926
0
104203
Swiss-Prot
-
NAPA_CAMFF
Campylobacter fetus subsp. fetus (strain 82-40)
925
0
104255
Swiss-Prot
-
NAPA_CAMHC
Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
920
0
103807
Swiss-Prot
-
NAPA_CAMJ8
Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
924
0
104900
Swiss-Prot
-
NAPA_CAMJE
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
924
0
104944
Swiss-Prot
-
NAPA_PSEA8
Pseudomonas aeruginosa (strain LESB58)
834
0
93484
Swiss-Prot
-
NAPA_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
834
0
93498
Swiss-Prot
-
NAPA_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
829
0
92975
Swiss-Prot
-
NAPA_RHOPB
Rhodopseudomonas palustris (strain BisB18)
837
0
93633
Swiss-Prot
-
NAPA_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
831
1
93164
Swiss-Prot
-
NAPA_SALAR
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
828
0
92847
Swiss-Prot
-
NAPA_SALCH
Salmonella choleraesuis (strain SC-B67)
828
0
92874
Swiss-Prot
-
NAPA_SALDC
Salmonella dublin (strain CT_02021853)
828
0
92890
Swiss-Prot
-
NAPA_SALEP
Salmonella enteritidis PT4 (strain P125109)
828
0
92874
Swiss-Prot
-
NAPA_SALG2
Salmonella gallinarum (strain 287/91 / NCTC 13346)
828
0
92872
Swiss-Prot
-
NAPA_SALHS
Salmonella heidelberg (strain SL476)
828
0
92874
Swiss-Prot
-
NAPA_SALPA
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
828
0
92858
Swiss-Prot
-
NAPA_CAMJJ
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
923
0
104771
Swiss-Prot
-
NAPA_CAMJR
Campylobacter jejuni (strain RM1221)
924
0
104944
Swiss-Prot
-
NAPA_CAMLR
Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
924
0
104803
Swiss-Prot
-
NAPA_CERS4
Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)
831
0
92637
Swiss-Prot
-
NAPA_CITK8
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
828
0
92994
Swiss-Prot
-
NAPA_COLP3
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
832
1
93469
Swiss-Prot
-
NAPA_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
831
0
93346
Swiss-Prot
-
NAPA_CUPPJ
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197)
831
0
93762
Swiss-Prot
-
NAPA_CUPTR
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1)
831
0
93381
Swiss-Prot
-
NAPA_DECAR
Dechloromonas aromatica (strain RCB)
837
0
93395
Swiss-Prot
-
NAPA_DESDA
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB)
755
1
83497
Swiss-Prot
-
NAPA_DINSH
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
831
0
92890
Swiss-Prot
-
NAPA_ECO24
Escherichia coli O139:H28 (strain E24377A / ETEC)
828
0
93130
Swiss-Prot
-
NAPA_ECO27
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
828
0
93067
Swiss-Prot
-
NAPA_ECO45
Escherichia coli O45:K1 (strain S88 / ExPEC)
828
0
93058
Swiss-Prot
-
NAPA_ECO55
Escherichia coli (strain 55989 / EAEC)
828
0
93026
Swiss-Prot
-
NAPA_ECO5E
Escherichia coli O157:H7 (strain EC4115 / EHEC)
828
0
93057
Swiss-Prot
-
NAPA_ECO7I
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
828
0
93116
Swiss-Prot
-
NAPA_ECOBW
Escherichia coli (strain K12 / MC4100 / BW2952)
828
0
93042
Swiss-Prot
-
NAPA_ECODH
Escherichia coli (strain K12 / DH10B)
828
0
93042
Swiss-Prot
-
NAPA_ECOL5
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
828
0
93070
Swiss-Prot
-
NAPA_ECOL6
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
828
0
93056
Swiss-Prot
-
NAPA_ECOLC
Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks)
828
0
93056
Swiss-Prot
-
NAPA_ECOLU
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
828
0
93056
Swiss-Prot
-
NAPA_ECOSM
Escherichia coli (strain SMS-3-5 / SECEC)
828
0
93070
Swiss-Prot
-
NAPA_ECOUT
Escherichia coli (strain UTI89 / UPEC)
828
0
93058
Swiss-Prot
-
NAPA_EDWI9
Edwardsiella ictaluri (strain 93-146)
829
0
92241
Swiss-Prot
-
NAPA_ESCF3
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73)
828
0
93056
Swiss-Prot
-
NAPA_GLAP5
Glaesserella parasuis serovar 5 (strain SH0165)
827
0
92969
Swiss-Prot
-
NAPA_HAEDU
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
827
0
93202
Swiss-Prot
-
NAPA_HAEI8
Haemophilus influenzae (strain 86-028NP)
827
0
93629
Swiss-Prot
-
NAPA_SALPB
828
0
92858
Swiss-Prot
-
NAPA_SALPC
Salmonella paratyphi C (strain RKS4594)
828
0
92890
Swiss-Prot
-
NAPA_SALPK
Salmonella paratyphi A (strain AKU_12601)
828
0
92858
Swiss-Prot
-
NAPA_SALSV
Salmonella schwarzengrund (strain CVM19633)
828
0
92888
Swiss-Prot
-
NAPA_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
828
0
92874
Swiss-Prot
-
NAPA_SERP5
Serratia proteamaculans (strain 568)
828
1
92599
Swiss-Prot
-
NAPA_SHEDO
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
829
0
93039
Swiss-Prot
-
NAPA_SHEHH
Shewanella halifaxensis (strain HAW-EB4)
826
0
92339
Swiss-Prot
-
NAPA_SHIB3
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
828
0
93058
Swiss-Prot
-
NAPA_SHIBS
Shigella boydii serotype 4 (strain Sb227)
828
0
93101
Swiss-Prot
-
NAPA_SHIDS
Shigella dysenteriae serotype 1 (strain Sd197)
828
0
93057
Swiss-Prot
-
NAPA_SHIF8
Shigella flexneri serotype 5b (strain 8401)
828
0
92989
Swiss-Prot
-
NAPA_SYMTH
Symbiobacterium thermophilum (strain T / IAM 14863)
754
0
83580
Swiss-Prot
-
NAPA_VIBC1
Vibrio campbellii (strain ATCC BAA-1116)
829
0
93061
Swiss-Prot
Mitochondrion (Reliability: 4)
NAPA_VIBC3
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
829
0
93106
Swiss-Prot
-
A0A725VNP3_SALEP
Salmonella enteritidis PT4 (strain P125109)
828
0
92858
TrEMBL
-
A0A426WHS5_SALET
828
0
92858
TrEMBL
-
A0A730JPZ9_SALET
828
0
92894
TrEMBL
-
A0A5W8MPH2_SALET
828
0
92874
TrEMBL
-
A0A5D0EKF0_AGGAC
828
0
93424
TrEMBL
-
A0A0H3PPY9_ECO5C
Escherichia coli O157:H7 (strain EC869)
828
0
93057
TrEMBL
-
A0A1Q4FQR5_9GAMM
830
0
92751
TrEMBL
-
A0A657I2S2_SALET
828
0
92874
TrEMBL
-
A0A828PZS7_ACTPL
819
0
92438
TrEMBL
-
A0A752MP43_SALHO
828
0
92883
TrEMBL
-
A0A5I0BQ31_SALET
828
0
92874
TrEMBL
-
I3XVX5_SULBS
Sulfurospirillum barnesii (strain ATCC 700032 / DSM 10660 / SES-3)
929
0
104497
TrEMBL
-
A0A5Y7AKZ5_SALIN
828
0
92864
TrEMBL
-
A0A1J5C2Q3_9BURK
840
1
93907
TrEMBL
-
A0A735KZ23_SALHO
828
0
92911
TrEMBL
-
A0A1S7U4W1_9HYPH
834
0
93349
TrEMBL
-
A0A833HJ11_9BACT
915
0
101023
TrEMBL
-
A0A5L4VYR4_CAMHY
923
0
104771
TrEMBL
-
A0A5Y2S3Z3_SALER
828
0
92830
TrEMBL
-
A0A259UGH5_9FIRM
753
0
83500
TrEMBL
-
A0A7C3Q895_9PROT
945
0
106790
TrEMBL
-
A0A1S2LG46_9BACI
862
0
97243
TrEMBL
-
A0A3V3U7I5_SALET
828
0
92874
TrEMBL
-
A0A3W0FJH3_SALET
828
0
92874
TrEMBL
-
A0A5J0NV81_SALET
828
0
92874
TrEMBL
-
A0A3V7IID4_SALET
828
0
92873
TrEMBL
-
A0A5I5Z330_SALET
828
0
92874
TrEMBL
-
A0A605YEU9_SALET
828
0
92888
TrEMBL
-
T0R4G0_AERSA
829
1
92827
TrEMBL
-
A0A410UVU7_9BURK
831
0
92950
TrEMBL
-
A0A1E2UKS2_9GAMM
856
0
95811
TrEMBL
-
A0A735PZ98_SALER
828
0
92874
TrEMBL
-
A0A5H7IQ99_SALET
828
0
92874
TrEMBL
-
A0A2M8DKU2_9BACT
832
0
93396
TrEMBL
-
A0A832N2S5_9GAMM
912
0
102934
TrEMBL
-
A0A7S7Q008_9BRAD
837
0
94416
TrEMBL
-
M1PJT4_DESSD
Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1)
772
0
86743
TrEMBL
-
D5UZL6_ARCNC
Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI)
940
0
106107
TrEMBL
-
A0A7S7U7R7_9BRAD
849
1
94927
TrEMBL
-
A0A0S8BLA3_9PROT
835
0
94090
TrEMBL
-
A0A1S2LRB6_9BACI
855
0
96818
TrEMBL
-
A0A659PBC7_SALET
828
0
92839
TrEMBL
-
A0A517SR88_9BACT
825
0
92141
TrEMBL
-
Q30QE0_SULDN
Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251)
940
0
105488
TrEMBL
-
A0A6J4X486_9DELT
771
0
86706
TrEMBL
-
A0A2N2SMJ8_9PROT
848
0
95017
TrEMBL
-
A0A1F9NZM3_9DELT
771
0
86589
TrEMBL
-
A0A1T4R040_9FIRM
786
0
87918
TrEMBL
-
A0A6C8EYK6_SALVI
828
0
92874
TrEMBL
-
A0A5I3I7A9_SALET
828
0
92874
TrEMBL
-
A0A7S7RQ66_9PROT
947
0
105640
TrEMBL
-
A0A655E908_SALET
774
0
87443
TrEMBL
-
A0A2K9P7V8_9ENTR
828
0
93003
TrEMBL
-
A0A8J6P117_9GAMM
848
0
94634
TrEMBL
-
A0A2U3QFA6_9BACT
154
1
17297
TrEMBL
-
A0A0F2Q0Z6_9CLOT
754
0
83449
TrEMBL
-
A0A2J6WKS8_9BACT
795
0
89569
TrEMBL
-
I0ENC0_HELC0
Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128)
950
0
108466
TrEMBL
-
A0A3Q8GH29_9PAST
832
0
94251
TrEMBL
-
A0A3Q9MSC3_SALET
828
0
92874
TrEMBL
-
A0A3V5IT04_SALET
828
0
92855
TrEMBL
-
A0A5W0RNL2_SALTM
828
0
92874
TrEMBL
-
A0A2M7HSA1_9GAMM
829
0
92816
TrEMBL
-
A0A2M7HPQ5_9GAMM
826
0
92312
TrEMBL
-
A0A6W0NYN2_SALRU
828
0
92874
TrEMBL
-
A0A239MAH8_CERSP
831
0
92663
TrEMBL
-
A3D8C5_SHEB5
Shewanella baltica (strain OS155 / ATCC BAA-1091)
831
0
93035
TrEMBL
-
A0A142BC31_9GAMM
834
0
94060
TrEMBL
-
A0A286BWS5_9ENTR
828
0
92499
TrEMBL
-
A0A6G7PYD1_9BACT
799
0
90366
TrEMBL
-
A0A0U1P731_PHOLE
828
0
93258
TrEMBL
-
K4KWM4_SIMAS
Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1)
828
0
92972
TrEMBL
-
A0A8E1WVN7_9PROT
839
0
93419
TrEMBL
-
A0A8J6N1I4_9DELT
750
0
83634
TrEMBL
-
A0A809NQ04_HELCP
Helicobacter cinaedi (strain PAGU611)
937
0
105400
TrEMBL
-
X2JS02_AGGAC
828
0
93492
TrEMBL
-
A0A735M7L7_SALER
828
0
92874
TrEMBL
-
A0A1H9P233_9BACI
853
0
96473
TrEMBL
-
A0A1P8EP76_9PSED
834
0
93842
TrEMBL
-
A3QHX4_SHELP
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
827
0
92169
TrEMBL
-
A0A0A8H2R1_9PROT
924
0
105001
TrEMBL
-
D5EKZ1_CORAD
Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865 / 04OKA010-24)
809
0
91107
TrEMBL
-
A0A518VJY1_PECCC
828
0
92701
TrEMBL
-
A0A0S8AFP8_9DELT
772
0
86860
TrEMBL
-
A0A5I8VCA4_SALET
828
0
92874
TrEMBL
-
A0A737NVN2_SALHO
828
0
92865
TrEMBL
-
A0A0T6VKW0_9PSED
834
0
93567
TrEMBL
-
A0A4P9DRK1_9PROT
942
0
107175
TrEMBL
-
A0A1T4S7J0_VIBCI
829
0
93230
TrEMBL
-
A0A5Y3UV78_SALER
828
0
92939
TrEMBL
-
A0A2U3QEF2_9BACT
923
0
104331
TrEMBL
-
A0A2T9QC45_SALET
828
0
92874
TrEMBL
-
A0A5J0NHW5_SALET
828
0
92888
TrEMBL
-
A0A5I1SI87_SALET
828
0
92874
TrEMBL
-
A0A3Z3GEC4_SALET
828
0
92821
TrEMBL
-
A0A0H3P0A8_YERE1
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
831
0
93432
TrEMBL
-
A0A836NBC0_ECOLX
828
0
93072
TrEMBL
-
D2MXR2_CAMJU
924
0
104894
TrEMBL
-
A0A2U1RGY5_9BACT
788
0
88593
TrEMBL
-
D0WFP5_SLAES
Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 / S-7)
854
0
94832
TrEMBL
-
A0A3L6LUI7_9RHOO
838
0
93564
TrEMBL
-
E3HM71_ACHXA
Achromobacter xylosoxidans (strain A8)
812
0
91261
TrEMBL
-
A0A753EJQ5_SALHO
828
0
92873
TrEMBL
-
G2SIM3_RHOMG
Rhodothermus marinus (strain SG0.5JP17-172)
756
0
84303
TrEMBL
-
A0A076LS52_9GAMM
829
0
92197
TrEMBL
-
A0A1G3D1D7_9GAMM
834
0
93610
TrEMBL
-
A0A5I6QS62_SALET
828
0
92874
TrEMBL
-
A0A5W0L9C1_SALET
828
0
92860
TrEMBL
-
A0A1Q3VNC2_9PROT
837
0
94212
TrEMBL
-
A0A2R8CA85_9RHOB
833
0
92899
TrEMBL
-
A0A1G2WCA5_9CAUL
830
0
91950
TrEMBL
-
A0A5B7XA77_9PROT
936
0
105818
TrEMBL
-
A0A5J0IPU9_SALET
828
0
92874
TrEMBL
-
A0A2M8E7I8_9BURK
842
0
93729
TrEMBL
-
A0A1Y5DVV2_9PROT
933
0
105218
TrEMBL
-
A0A737LZ93_SALHO
828
0
92839
TrEMBL
-
A0A806HHX5_PSEST
834
0
93859
TrEMBL
-
A0A5W3F5E7_SALET
828
0
92864
TrEMBL
-
A0A1E7HHF0_9DELT
772
0
87026
TrEMBL
-
A0A517NXZ6_9BACT
806
0
90213
TrEMBL
-
A0A728LPA3_SALER
828
0
92874
TrEMBL
-
A0A5I2UUN6_SALET
828
0
92874
TrEMBL
-
A0A1Y5HL18_9RHOB
834
0
92597
TrEMBL
-
A0A730W9G6_SALHO
828
0
92874
TrEMBL
-
B2V808_SULSY
Sulfurihydrogenibium sp. (strain YO3AOP1)
934
0
106341
TrEMBL
-
A0A0X8NX36_ALCXX
831
0
93395
TrEMBL
-
A0A7U1Q9E8_SALET
828
0
92874
TrEMBL
-
A0A828QV52_CAMUP
924
0
104985
TrEMBL
-
C3MA13_SINFN
Sinorhizobium fredii (strain NBRC 101917 / NGR234)
843
0
94212
TrEMBL
-
A0A0M2U4C2_9FIRM
749
0
82424
TrEMBL
-
A0A0A7MHX9_ACTEU
827
0
93364
TrEMBL
-
A0A5H9YC33_SALET
828
0
92874
TrEMBL
-
A0A5X6EUH3_SALET
828
0
92874
TrEMBL
-
A0A517TGH5_9BACT
805
0
89884
TrEMBL
-
A0A6H0T3J4_9PAST
827
0
92864
TrEMBL
-
A0A724L9W4_SALEP
Salmonella enteritidis PT4 (strain P125109)
828
0
92908
TrEMBL
-
A0A258X1Q7_9PROT
929
0
104824
TrEMBL
-
A0A6G8ZQT1_9BRAD
837
0
93964
TrEMBL
-
D0ME93_RHOM4
Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10)
762
0
85037
TrEMBL
-
A0A6C8G8Y6_SALIN
828
0
92864
TrEMBL
-
A0A8E7QPR7_SALET
828
0
92874
TrEMBL
-
A0A1M5P393_9PSED
834
0
93501
TrEMBL
-
A0A257FNE0_9BURK
848
0
94649
TrEMBL
-
A0A1W1WQM5_9PROT
936
0
106357
TrEMBL
-
A0A259UUN3_9FIRM
753
0
83494
TrEMBL
-
A0A1Y1R921_9PROT
936
0
105455
TrEMBL
-
E6X8F3_CELAD
Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630)
775
0
86948
TrEMBL
-
A0A1M7YCY3_9DELT
784
1
88397
TrEMBL
-
A0A0C2BNI4_9BURK
832
0
93141
TrEMBL
-
A0A7X8YL77_9VIBR
829
0
92928
TrEMBL
-
A0A2N2QY43_9PROT
847
0
94594
TrEMBL
-
C0QTS6_PERMH
Persephonella marina (strain DSM 14350 / EX-H1)
946
0
108112
TrEMBL
-
A0A5B8XTA5_9DELT
799
0
89992
TrEMBL
-
A0A532UW34_9BACT
866
0
96820
TrEMBL
-
A0A735VRJ0_SALDZ
828
0
92882
TrEMBL
-
A0A729ZWW7_SALET
828
0
92858
TrEMBL
-
A0A8E6NAZ1_SALTM
828
0
92874
TrEMBL
-
E4TGR3_CALNY
Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1)
795
0
89511
TrEMBL
-
A0A0A8HZ39_CAMLA
924
0
104750
TrEMBL
-
A0A0A8GST2_9PROT
924
0
104966
TrEMBL
-
A0A1J5BKR3_9PROT
838
0
93965
TrEMBL
-
I2NMT2_9PAST
833
0
94324
TrEMBL
-
A0A024HFA2_PSEKB
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
834
0
93087
TrEMBL
-
S3XAJ8_9PROT
927
0
105116
TrEMBL
-
A0A5H9WYJ8_SALET
828
0
92874
TrEMBL
-
A0A6C7IDY1_SALTD
Salmonella typhimurium (strain D23580)
828
0
92874
TrEMBL
-
A0A735W7Q6_SALET
828
0
92805
TrEMBL
-
A0A2T4TUR8_9BACT
789
0
87856
TrEMBL
-
A0A7H9CG75_9PROT
923
0
104303
TrEMBL
-
A0A5X7K2I9_SALET
828
0
92874
TrEMBL
-
A0A5V9GNN7_SALET
828
0
92858
TrEMBL
-
N6Z8E7_THAL4
Thauera linaloolentis (strain DSM 12138 / CCUG 41526 / CIP 105981 / IAM 15112 / NBRC 102519 / 47Lol)
848
0
95011
TrEMBL
-
A0A1H5FJB1_9PSED
834
0
93856
TrEMBL
-
A0A2T6NB08_9GAMM
856
0
95873
TrEMBL
-
A0A0K1HF25_9PROT
927
0
104988
TrEMBL
-
A0A752RV67_SALET
828
0
92888
TrEMBL
-
V1H3X5_SALER
828
0
92888
TrEMBL
-
A0A0A8HBJ3_9PROT
924
0
104787
TrEMBL
-
A0A1W6BWS0_9PROT
922
0
104670
TrEMBL
-
A0A739C8L9_SALER
828
0
92847
TrEMBL
-
A0A0C1ZCB9_9VIBR
829
0
93074
TrEMBL
-
A0A7U7ISE9_YEREN
831
0
93416
TrEMBL
-
A0A737ET11_SALER
828
0
92847
TrEMBL
-
A0A1S7QHT0_RHIRD
834
0
93412
TrEMBL
-
A0A1J5FIK9_9HELI
948
0
106505
TrEMBL
-
A0A5W2LSW7_SALET
828
0
92874
TrEMBL
-
A0A5I0SK35_SALET
828
0
92874
TrEMBL
-
A0A3V4SLC6_SALET
828
0
92874
TrEMBL
-
A0A3V5VQV4_SALET
828
0
92874
TrEMBL
-
A0A5T5IDQ6_SALET
828
0
92858
TrEMBL
-
A0A8E6S0K9_SALER
828
0
92874
TrEMBL
-
A0A2A3LKM1_9GAMM
832
0
92970
TrEMBL
-
A0A367UGJ5_9PROT
834
0
94055
TrEMBL
-
A0A7G9YTN1_9EURY
81
0
9267
TrEMBL
-
A0A7G9YZY5_9EURY
117
0
13429
TrEMBL
-
A0A7G9YZL5_9EURY
163
0
18554
TrEMBL
-
A0A085G852_9ENTR
828
0
92736
TrEMBL
-
I3YGE0_THIV6
Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111)
858
0
97116
TrEMBL
-
A0A5N4FMB3_PHODD
828
0
93250
TrEMBL
-
A0A732CXB3_SALER
828
0
92874
TrEMBL
-
A0A0S4RLC8_CAMFE
926
0
104196
TrEMBL
-
A0A1F4LES4_9BURK
840
0
93881
TrEMBL
-
A0A0E0UKY6_SINMB
Sinorhizobium meliloti (strain BL225C)
834
0
93247
TrEMBL
-
A0A137SAX7_9GAMM
834
0
93954
TrEMBL
-
A0A2S0QZ73_9RHOO
851
0
95093
TrEMBL
-
A0A2K9NL56_9PROT
833
0
93166
TrEMBL
-
A0A564ZH30_9BACT
788
0
88310
TrEMBL
-
A0A2N2QA22_9PROT
837
0
93085
TrEMBL
-
A0A726XRP2_SALET
828
0
92888
TrEMBL
-
Q1ZPL7_PHOAS
Photobacterium angustum (strain S14 / CCUG 15956)
828
0
93314
TrEMBL
-
A0A6N3J4M3_SHESW
Shewanella sp. (strain W3-18-1)
829
0
92797
TrEMBL
-
A0A8E0N6E7_ECOLX
828
0
93072
TrEMBL
-
B8G227_DESHD
Desulfitobacterium hafniense (strain DSM 10664 / DCB-2)
758
0
83387
TrEMBL
-
A0A850F655_9ENTR
828
0
92558
TrEMBL
-
Q080C0_SHEFN
Shewanella frigidimarina (strain NCIMB 400)
829
0
93099
TrEMBL
-
A0A1B7JLI1_9GAMM
828
0
92715
TrEMBL
-
A0A1M7XVD1_9DELT
796
0
88912
TrEMBL
-
A0A5U3DMH8_SALER
828
0
93011
TrEMBL
-
A0A5Y3MN79_SALER
828
0
92888
TrEMBL
-
A0A497TK57_9BACT
857
0
96385
TrEMBL
-
A0A8J6TN58_9GAMM
853
0
95719
TrEMBL
-
A0A2N2QTX9_9PROT
837
0
93517
TrEMBL
-
A0A367W099_9PROT
834
0
94243
TrEMBL
-
A0A0J6YVT1_9BACT
799
0
89798
TrEMBL
-
A0A6W0M2E1_SALET
828
0
92874
TrEMBL
-
A0A4P9T452_SALET
828
0
92830
TrEMBL
-
A0A8J6Y1L5_9BACT
Candidatus Polarisedimenticola svalbardensis
916
0
101850
TrEMBL
Mitochondrion (Reliability: 4)
A0A4Q0XTW4_9PROT
Candidatus Marinarcus aquaticus
936
0
105364
TrEMBL
-
E1W407_HAEP3
Haemophilus parainfluenzae (strain T3T1)
828
0
93676
TrEMBL
-
A0A3V8VP41_SALET
828
0
92874
TrEMBL
-
A0A5Y0UYB7_SALET
828
0
92850
TrEMBL
-
A0A3V9PTA8_SALET
828
0
92864
TrEMBL
-
A0A718R3H8_SALTS
Salmonella typhimurium (strain SL1344)
828
0
92858
TrEMBL
-
A0A7H4ZN02_YERP4
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain YE-P4)
831
0
93432
TrEMBL
-
A0A729QL36_SALET
828
0
92900
TrEMBL
-
A0A1R1JW30_ALCXX
831
0
93424
TrEMBL
-
A0A2R4TUC0_AERHY
829
0
92798
TrEMBL
-
A0A0C2UAZ5_MAGMG
827
0
93002
TrEMBL
-
A0A2U0T889_9PAST
827
0
93182
TrEMBL
-
A0A2M7Y0I3_9RHOO
838
0
93965
TrEMBL
-
A0A733VD64_SALET
828
0
92890
TrEMBL
-
A0A719CTP1_SALTS
Salmonella typhimurium (strain SL1344)
828
0
92888
TrEMBL
-
A0A1I1E2A8_9GAMM
828
0
93296
TrEMBL
-
A0A1S7RGG3_9HYPH
834
0
93444
TrEMBL
-
A0A6M8J6S0_9ACTN
846
1
93041
TrEMBL
-
A0A855N340_CAMHY
926
0
104210
TrEMBL
-
A0A249PRI5_RHIFR
834
0
93324
TrEMBL
-
A0A822V775_RHIRD
834
0
93558
TrEMBL
-
M7RD46_SALDU
828
0
92890
TrEMBL
-
A0A8F8DPT2_9ESCH
828
0
93042
TrEMBL
-
A0A737NA92_SALET
828
0
92831
TrEMBL
-
A0A5I6NMS1_SALET
828
0
92874
TrEMBL
-
A0A844CNA8_9ENTR
828
0
92785
TrEMBL
-
A0A5I0YX68_SALET
828
0
92874
TrEMBL
-
A0A2U8QH13_9BRAD
837
0
94008
TrEMBL
-
D3P985_DEFDS
Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 / SSM1)
795
0
89760
TrEMBL
-
A0A5I2Z0J8_SALET
828
0
92874
TrEMBL
-
K4X2M7_ECOLX
828
0
93072
TrEMBL
-
A0A837DRS9_PECCC
828
0
92769
TrEMBL
-
A0A0K0HCK5_SALBC
Salmonella bongori (strain ATCC 43975 / DSM 13772 / NCTC 12419)
828
0
93011
TrEMBL
-
V7IJU3_SALET
828
0
92874
TrEMBL
-
A0A636KCW6_SALET
828
0
92874
TrEMBL
-
A0A661WXR0_9BACT
755
0
84319
TrEMBL
-
A0A1G7M0F9_9FIRM
755
0
83918
TrEMBL
-
A0A1X4MRY8_9PROT
834
0
94182
TrEMBL
-
A0A1F2Q957_9BACT
789
0
88111
TrEMBL
-
A1S623_SHEAM
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
831
0
93167
TrEMBL
-
A0A1P8FPM2_9PROT
842
0
94176
TrEMBL
-
A0A370DP17_9GAMM
857
0
96214
TrEMBL
-
E4U737_OCEP5
Oceanithermus profundus (strain DSM 14977 / NBRC 100410 / VKM B-2274 / 506)
938
0
105876
TrEMBL
-
A0A1X9SNA5_9PROT
925
0
104228
TrEMBL
-
A0A1J5DZE5_9DELT
905
0
102198
TrEMBL
-
A0A1I1J5E1_9RHOB
835
0
93521
TrEMBL
-
A0A1S2LE67_9BACI
856
0
96757
TrEMBL
-
A0A418ZCG7_SALET
828
0
92874
TrEMBL
-
A0A5J1II38_SALET
828
0
92874
TrEMBL
-
A0A5W8CAN6_SALET
828
0
92874
TrEMBL
-
A0A5J1A5E2_SALET
828
0
92874
TrEMBL
-
A0A5I9RMD2_SALET
828
0
92874
TrEMBL
-
A0A0S8BDK8_9PROT
831
0
92528
TrEMBL
-
L0DVG7_THIND
Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2)
913
0
102712
TrEMBL
-
A0A1F4KHL8_9BURK
840
0
93979
TrEMBL
-
A0A2N2TWH8_9PROT
846
0
94166
TrEMBL
-
A0A2C9NXL7_SALET
828
0
92816
TrEMBL
-
A0A7C3CW18_9GAMM
915
0
103449
TrEMBL
-
A0A718RL41_SALTS
Salmonella typhimurium (strain SL1344)
828
0
92864
TrEMBL
-
A0NZM8_ROSAI
Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM 12614 / B1)
831
0
92588
TrEMBL
-
A0A829QWD7_9GAMM
828
0
92781
TrEMBL
-
A0A0C5W4T1_9GAMM
828
0
93065
TrEMBL
-
A0A5I8HSF5_SALET
828
0
92874
TrEMBL
-
W0R9H2_BIBTR
827
0
93412
TrEMBL
-
A0A177E818_9BACT
800
0
90289
TrEMBL
-
A0A1E5BB69_9VIBR
828
0
92923
TrEMBL
-
A0A353V9K9_9BACT
784
0
87412
TrEMBL
-
L0F694_DESDL
Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1)
758
0
83820
TrEMBL
-
A0A4V7I8B6_BIBTR
827
0
93428
TrEMBL
-
A0A1F2V8J7_9BACT
848
0
94260
TrEMBL
-
E6WPJ6_PSEUU
Pseudoxanthomonas suwonensis (strain 11-1)
831
0
93134
TrEMBL
-
A0A6N3J1R0_SHESW
Shewanella sp. (strain W3-18-1)
826
0
92335
TrEMBL
-
A0A737BHU0_SALER
828
0
92888
TrEMBL
-
A0A5Y3AZV0_SALER
828
0
92855
TrEMBL
-
E7A8R0_HELFC
Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1)
939
0
106246
TrEMBL
-
R5EF58_9BURK
921
0
103158
TrEMBL
-
A0A5H9VKI2_SALET
828
0
92874
TrEMBL
-
A0A2N7W0R1_9BURK
1417
0
153832
TrEMBL
-
A0A3Z6QGT4_SALET
828
0
92888
TrEMBL
-
A0A5C5HDH4_SALET
828
0
92874
TrEMBL
-
A0A736URC5_SALET
828
0
92888
TrEMBL
-
A0A2T9I7E8_SALET
828
0
92874
TrEMBL
-
A0A715JGR0_SALTI
828
0
92858
TrEMBL
-
A0A637CR32_SALET
828
0
92874
TrEMBL
-
D3UIN9_HELM1
Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
927
0
105170
TrEMBL
-
A0A730K590_SALHO
828
0
92883
TrEMBL
-
A0A8F9Z195_SALET
828
0
92874
TrEMBL
-
A0A143XBG9_9ACTN
846
0
93676
TrEMBL
-
A0A7G9YQV5_9EURY
187
0
20729
TrEMBL
-
A0A1G1HT63_9BACT
841
0
94441
TrEMBL
-
A0A6J5GJS0_9BURK
1400
0
151439
TrEMBL
-
B5ZZF8_RHILW
Rhizobium leguminosarum bv. trifolii (strain WSM2304)
835
0
93286
TrEMBL
-
A0A2M7MU82_9PROT
919
0
103012
TrEMBL
-
A0A3P1XLP7_9BURK
844
0
94993
TrEMBL
-
A0A2P7B6A4_9HYPH
833
0
93511
TrEMBL
-
A0A1W9STE7_9BACT
929
0
105201
TrEMBL
-
A0A5W7BD91_SALET
828
0
92846
TrEMBL
-
A0A0F6B3Y8_SALT1
Salmonella typhimurium (strain 14028s / SGSC 2262)
828
0
92860
TrEMBL
-
I4CB25_DESTA
Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1)
797
0
88938
TrEMBL
-
Q1LFZ5_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
831
0
93725
TrEMBL
-
A0A0H3PDV8_HAEI3
Haemophilus influenzae (strain NTHi 3655)
827
0
93687
TrEMBL
-
E6X0K6_NITSE
Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1)
944
0
107070
TrEMBL
-
A0A1G1FDB3_9BACT
922
0
103171
TrEMBL
-
A0A2A5AAV7_9BACT
800
0
89971
TrEMBL
-
A0A731TCQ9_SALEE
828
0
92880
TrEMBL
-
A0A1S7LIG9_MAGMO
Magnetococcus massalia (strain MO-1)
836
0
94481
TrEMBL
-
A0A1G3TAK4_9PROT
940
0
105295
TrEMBL
-
A0A8E7RBP5_SALET
828
0
92874
TrEMBL
-
A0A2T4V6G5_VITXG
Vitiosangium sp. (strain GDMCC 1.1324)
806
0
90202
TrEMBL
-
A0A1F2SYQ1_9BACT
848
0
94015
TrEMBL
-
Q088A1_SHEFN
Shewanella frigidimarina (strain NCIMB 400)
827
0
92053
TrEMBL
-
A0A7H7GFF7_CAMHY
925
0
104243
TrEMBL
-
A0A7I9K8B8_CAMHY
924
0
105072
TrEMBL
-
A0A2N2R5X9_9PROT
837
0
93085
TrEMBL
-
A0A6V9XJP9_SALET
828
0
92902
TrEMBL
-
A0A1S6TMI9_9PROT
925
0
104482
TrEMBL
-
A0A1W9QV53_9BACT
928
0
104297
TrEMBL
-
A0A5C4PXA2_9PAST
826
0
93362
TrEMBL
-
A0A1W1UFN5_9PAST
826
0
93337
TrEMBL
-
A4AMZ6_MARSH
Maribacter sp. (strain HTCC2170 / KCCM 42371)
775
0
87157
TrEMBL
-
A0A8F2ZW30_SALET
828
0
92874
TrEMBL
-
A0A3V8D675_SALET
828
0
92874
TrEMBL
-
A0A5J1BYL5_SALET
828
0
92874
TrEMBL
-
A0A3T2ZTU8_SALET
828
0
92888
TrEMBL
-
A0A379S2I2_SALER
828
0
92847
TrEMBL
-
A0A5I0B7W5_SALET
828
0
92888
TrEMBL
-
A0A737P9H0_SALET
828
0
92874
TrEMBL
-
A0A1D7Z7C6_9GAMM
828
0
92759
TrEMBL
-
A0A557S7P8_9GAMM
853
0
95339
TrEMBL
-
D2AF12_SHIF2
Shigella flexneri serotype X (strain 2002017)
828
0
92987
TrEMBL
-
A0A011QHN8_ACCSB
Accumulibacter sp. (strain BA-93)
841
0
93647
TrEMBL
-
A0A6G5QGG4_9PROT
927
0
104713
TrEMBL
-
A0A7G9YQV4_9EURY
195
0
21674
TrEMBL
-
A0A5X9FG56_SALET
828
0
92902
TrEMBL
-
A0A1L9QBW8_9PROT
830
0
92741
TrEMBL
-
A0A8E0SL61_PHODD
828
0
93298
TrEMBL
-
A0A731V667_SALET
828
0
92888
TrEMBL
-
A0A1F7NTL1_9BACT
784
0
87302
TrEMBL
-
E1SPK7_FERBD
Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT)
826
0
92214
TrEMBL
-
I0ET59_HELCM
Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656)
943
0
107313
TrEMBL
-
V9VXK3_9RHOB
832
0
93222
TrEMBL
-
A0A6C7C2U4_SALER
828
0
92925
TrEMBL
-
A0A2K9NJA7_9PROT
833
0
93190
TrEMBL
-
A0A714B9W7_SALTI
828
0
92848
TrEMBL
-
A0A1G0N0Z7_9DELT
772
0
86180
TrEMBL
-
A0A6J5FJJ1_9BURK
827
0
92492
TrEMBL
-
A0A1G7N206_9PSED
834
0
93623
TrEMBL
-
A0A140NG77_PROSM
Providencia stuartii (strain MRSN 2154)
828
0
93088
TrEMBL
-
A0A7S7UMK2_9BRAD
837
0
94370
TrEMBL
-
A0A511QFU5_9VIBR
828
0
93638
TrEMBL
-
A0A518L1J2_9BACT
805
0
89799
TrEMBL
-
D4H1E4_DENA2
Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460)
797
0
88667
TrEMBL
-
E0IY97_ECOLW
Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB 8666 / NRRL B-766 / W)
828
0
93026
TrEMBL
-
A0A0A6PC10_9GAMM
835
0
94582
TrEMBL
-
A0A7U7FV21_YEREN
831
0
93432
TrEMBL
-
A0A730TTK2_SALET
828
0
92874
TrEMBL
-
A0A3V7KN14_SALET
828
0
92874
TrEMBL
-
A0A5I3RAN4_SALET
828
0
92874
TrEMBL
-
A0A265B8E3_SALET
828
0
92874
TrEMBL
-
A0A5Y0MPE7_SALET
828
0
92864
TrEMBL
-
A0A8E6NSS8_SALET
828
0
92858
TrEMBL
-
E0UTD4_SULAO
Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10)
948
0
106904
TrEMBL
-
A0A3N0AXZ3_9ACTN
846
0
93018
TrEMBL
-
A0A1W9UCD0_9DELT
800
0
89783
TrEMBL
-
W0Q8A8_9PAST
836
0
94555
TrEMBL
-
A0A737XZQ0_SALER
828
0
92883
TrEMBL
-
A0A1D7TIG1_9PROT
929
0
104228
TrEMBL
-
A0A6X7U398_SALET
828
0
92926
TrEMBL
-
F8AE26_THEID
Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812)
800
0
90355
TrEMBL
-
A0A483A9S8_9GAMM
847
0
95409
TrEMBL
-
A0A3T0SEZ6_9GAMM
834
0
93756
TrEMBL
-
A0A727YWC1_SALHO
828
0
92883
TrEMBL
-
A0A5U9IEA0_SALET
828
0
92888
TrEMBL
-
A0A8E9YH94_SALDZ
828
0
92912
TrEMBL
-
E3PDQ8_ECOH1
Escherichia coli O78:H11 (strain H10407 / ETEC)
828
0
93074
TrEMBL
-
A0A1B7HNK0_9ENTR
828
0
92729
TrEMBL
-
E1SPL1_FERBD
Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT)
826
0
91972
TrEMBL
-
A0A6S7B402_9BURK
1397
0
151316
TrEMBL
-
A0A1G3TML9_9PROT
940
0
105677
TrEMBL
-
A0A6J5FBC8_9BURK
1395
0
150887
TrEMBL
-
A0A657FPY3_SALET
828
0
92830
TrEMBL
-
A0A5H7S1P3_SALET
828
0
92874
TrEMBL
-
G4A8U9_AGGAC
828
0
93447
TrEMBL
-
A0A602Z1X9_SALET
828
0
92902
TrEMBL
-
A1BB88_PARDP
Paracoccus denitrificans (strain Pd 1222)
831
0
92690
TrEMBL
-
A0A562XC10_CAMHY
925
0
104243
TrEMBL
-
A0A7Y5KEJ8_9BACT
781
0
87356
TrEMBL
-
A0A5Y2LNI9_SALER
828
0
92888
TrEMBL
-
A0A7S7LWE0_9PROT
947
0
105579
TrEMBL
-
A0A6C8LPM0_SALET
828
0
92874
TrEMBL
-
W6RHN5_PSEP5
Pseudomonas pseudoalcaligenes (strain CECT 5344)
834
0
93563
TrEMBL
-
A0A661I535_9PROT
942
0
105856
TrEMBL
-
A0A3V5UJT0_SALET
828
0
92888
TrEMBL
-
A0A344R034_SALER
828
0
92883
TrEMBL
-
A0A0H3NNR2_SALTS
Salmonella typhimurium (strain SL1344)
828
0
92874
TrEMBL
-
A0A5H5XID9_SALET
828
0
92874
TrEMBL
-
A0A3Q9L573_SALET
828
0
92874
TrEMBL
-
A0A511RLB6_9DEIN
938
0
105984
TrEMBL
-
A0A2N2S055_9PROT
793
0
88644
TrEMBL
-
A0A176XQA1_ALCXX
831
0
93042
TrEMBL
-
A0A424W6K4_ALCXX
831
0
93322
TrEMBL
-
A0A4Q0ZX32_9PROT
936
0
105823
TrEMBL
-
K0MJ79_BORPB
Bordetella parapertussis (strain Bpp5)
831
0
93168
TrEMBL
-
A0A6C7DBP6_SALER
828
0
92883
TrEMBL
-
A0A6N0HRM8_9GAMM
853
0
94761
TrEMBL
-
A0A609WB21_SALET
828
0
92858
TrEMBL
-
G8Q491_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
834
0
93823
TrEMBL
-
A0A855N9I6_CAMHY
926
0
104266
TrEMBL
-
B1KH54_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
826
0
92553
TrEMBL
-
A0A074JV30_9PROT
834
0
94082
TrEMBL
-
A0A1J5DI27_9DELT
916
0
101997
TrEMBL
-
A0A2N2ABG9_9GAMM
857
0
96003
TrEMBL
-
A0A2A3VLX4_9GAMM
832
0
93038
TrEMBL
-
A0A421K7H7_9GAMM
856
0
95895
TrEMBL
-
A0A737RMM1_SALET
828
0
92874
TrEMBL
-
A0A0M3TUH7_9GAMM
847
0
95669
TrEMBL
-
A0A0H3DRS3_EDWTF
Edwardsiella tarda (strain FL6-60)
829
0
92280
TrEMBL
-
A0A444H2C4_9GAMM
841
0
94501
TrEMBL
-
A0A1Q3VCB0_9PROT
833
0
92833
TrEMBL
-
A0A1I3S9D9_9HYPH
833
0
93260
TrEMBL
-
A0A1G3DHI7_9GAMM
834
0
93699
TrEMBL
-
A0A6I2IHR8_9ENTR
828
0
92619
TrEMBL
-
A0A2N2UPR0_9PROT
848
0
94859
TrEMBL
-
A0A7C9UY43_9PROT
834
0
93853
TrEMBL
-
E4U153_SULKY
Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1)
928
0
104623
TrEMBL
-
E4U3J9_SULKY
Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1)
928
0
104258
TrEMBL
-
A0A5Y2QSV8_SALER
828
0
92883
TrEMBL
-
A0A6J4YK38_9DELT
771
0
86764
TrEMBL
-
A0A0A5HTF8_PHOS4
Photobacterium sp. (strain ATCC 43367)
829
0
92882
TrEMBL
-
A0A3S4PYS6_AGGAP
826
0
93258
TrEMBL
-
A0A1J5N6R0_9GAMM
830
0
93334
TrEMBL
-
A0A5V8Y0E1_SALET
828
0
92858
TrEMBL
-
A0A7V1H8P0_9BACT
799
0
90129
TrEMBL
-
A0A1T4UQL3_9GAMM
828
0
92099
TrEMBL
-
A0A4R1BGZ6_9PROT
917
0
103398
TrEMBL
-
D3H0P6_ECO44
Escherichia coli O44:H18 (strain 042 / EAEC)
828
0
93056
TrEMBL
-
A0A644U1K5_9ZZZZ
758
0
83387
TrEMBL
Mitochondrion (Reliability: 5)
A0A4Q8PGZ0_SALET
828
0
92874
TrEMBL
-
A0A5I0RSS9_SALET
828
0
92874
TrEMBL
-
A0A5Y3KYU6_SALET
828
0
92888
TrEMBL
-
A0A5Z8R0E0_SALET
828
0
92860
TrEMBL
-
A0A369P292_9ACTN
846
0
93022
TrEMBL
-
A0A1G3HD75_9RHOO
849
0
95001
TrEMBL
-
F8GSA2_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
831
0
93413
TrEMBL
-
A0A011P2G0_9PROT
841
0
93842
TrEMBL
-
A0A6G8J5P6_9PAST
827
0
93304
TrEMBL
-
A0A8E6RRX3_SALET
828
0
92902
TrEMBL
-
A0A7Z2PQQ6_9BRAD
831
0
92344
TrEMBL
-
A0A5W7RX56_SALET
828
0
92874
TrEMBL
-
A0A8E5JNW7_SALEN
828
0
92874
TrEMBL
-
A0A5I5SSX4_SALET
828
0
92858
TrEMBL
-
A0A0J6YPU0_9BACT
799
0
89798
TrEMBL
-
D0YZC9_PHODD
820
0
92264
TrEMBL
-
A0A6G9A5R8_9BRAD
837
0
94024
TrEMBL
-
A0A0E0XWN5_ECO1C
Escherichia coli O104:H4 (strain 2011C-3493)
828
0
93026
TrEMBL
-
A0A2T6NCR1_9GAMM
856
0
95971
TrEMBL
-
A0A4Q9JW10_9PROT
922
0
105187
TrEMBL
-
A0A6N3LH05_9VIBR
829
0
93130
TrEMBL
-
A0A1C3RJ51_9PROT
836
0
94139
TrEMBL
-
A0A6J5BSP6_9BURK
1400
0
151418
TrEMBL
-
F8KST2_HELBC
Helicobacter bizzozeronii (strain CIII-1)
942
0
106719
TrEMBL
-
A0A1F6G4U3_9PROT
911
0
101623
TrEMBL
-
A0A6J5GK82_9BURK
1394
0
152469
TrEMBL
-
A0A254TDB9_9BURK
832
0
93080
TrEMBL
-
A0A1J5LR51_9BACT
774
1
87634
TrEMBL
-
A0A5C2QZ22_HAEIF
827
0
93639
TrEMBL
-
A0A4D6P5A2_SALET
828
0
92874
TrEMBL
-
A0A0E3V4Z5_PASMD
828
0
93262
TrEMBL
-
A0A5Y7A4J4_SALET
828
0
92874
TrEMBL
-
A0A1X0XXH2_9DELT
773
0
86670
TrEMBL
-
A0A379NHC5_SALET
828
0
92874
TrEMBL
-
A0A5V8AIK1_SALET
828
0
92874
TrEMBL
-
A0A5I8FRZ8_SALET
828
0
92874
TrEMBL
-
A0A3U7ZLB5_SALET
828
0
92880
TrEMBL
-
A0A2T8XE68_SALET
828
0
92874
TrEMBL
-
A0A2Z3FT25_RHIFR
834
0
93270
TrEMBL
-
F2NPN8_MARHT
Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1)
943
0
106991
TrEMBL
-
A0A2U1S0G5_9BACT
788
0
88503
TrEMBL
-
A0A1Z7YZX2_9FLAO
774
0
86658
TrEMBL
-
A8ERQ9_ALIB4
Aliarcobacter butzleri (strain RM4018)
936
0
105626
TrEMBL
-
A0A702BTM5_SALBN
828
0
93011
TrEMBL
-
A0A5V6PY84_SALET
828
0
92874
TrEMBL
-
A0A0C5WNZ5_9GAMM
830
0
93286
TrEMBL
-
B1KIA5_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
831
0
93356
TrEMBL
-
C8WHW3_EGGLE
Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B)
854
0
94798
TrEMBL
-
A0A1L3L1Y6_9HYPH
834
0
93386
TrEMBL
-
A0A1B7IM62_9ENTR
828
0
92742
TrEMBL
-
A0A701ULR0_SALER
828
0
92942
TrEMBL
-
A0A5I0D2K5_SALET
828
0
92874
TrEMBL
-
A0A654CPI6_9GAMM
828
0
92800
TrEMBL
-
S6AB21_SULDS
Sulfuricella denitrificans (strain DSM 22764 / NBRC 105220 / skB26)
841
0
93991
TrEMBL
-
U1QH17_9PAST
819
0
92360
TrEMBL
-
A0A658IJW1_SALNE
828
0
92874
TrEMBL
-
A0A5C7KRG4_9BACT
808
0
90546
TrEMBL
-
A0A1S2LTX0_9BACI
855
0
96550
TrEMBL
-
A0A2I3CP40_VIBAX
Vibrio alginolyticus (strain ATCC 17749 / DSM 2171 / NBRC 15630 / NCIMB 1903 / NCTC 12160 / XII-53)
829
0
93206
TrEMBL
-
A0A5C4PQD2_9PAST
826
0
93376
TrEMBL
-
A0A2R4MY73_9FIRM
786
0
87918
TrEMBL
-
A0A2M7WQN7_9PROT
837
1
94370
TrEMBL
-
A0A0M9F9S0_PHOLD
828
0
93244
TrEMBL
-
A0A8G2BFP9_9PROT
834
0
93817
TrEMBL
-
C7N4I0_SLAHD
Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1)
851
0
95217
TrEMBL
-
A0A3D8HY65_9HELI
930
0
105059
TrEMBL
-
V4NH05_PASMD
830
0
93615
TrEMBL
-
A0A085A9I1_9ENTR
828
0
92758
TrEMBL
-
F8H2N4_PSEUT
Pseudomonas stutzeri (strain ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 / NBRC 14165 / NCIMB 11358 / Stanier 221)
834
0
93726
TrEMBL
-
A0A2S0JDA1_CAMFE
925
0
104151
TrEMBL
-
A0A2H0HTL7_9GAMM
830
0
92373
TrEMBL
-
H1LQV0_9PAST
819
0
92369
TrEMBL
-
A0A8B2QZP4_CAMHY
925
0
104203
TrEMBL
-
A0A5I0EVC4_SALET
828
0
92874
TrEMBL
-
F7YR77_VIBA7
Vibrio anguillarum (strain ATCC 68554 / 775)
829
0
92994
TrEMBL
-
A0A323UT26_9RHOO
848
0
95134
TrEMBL
-
I4A6R6_DESDJ
Desulfitobacterium dehalogenans (strain ATCC 51507 / DSM 9161 / JW/IU-DC1)
758
0
83799
TrEMBL
-
A0A423UIG1_9ACTN
856
0
94691
TrEMBL
-
A0A0B6U490_CAMJU
924
0
104944
TrEMBL
-
A0A735JS20_SALPA
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
828
0
92858
TrEMBL
-
B6BKQ7_SULGG
Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1)
939
0
105697
TrEMBL
-
A0A809RR34_9PROT
847
0
94809
TrEMBL
-
A0A0S3QRC3_THET7
Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6)
802
0
90354
TrEMBL
-
A0A729JS82_SALER
828
0
92883
TrEMBL
-
A0A2T8L1D0_SALET
828
0
92874
TrEMBL
-
A0A315GQE7_SALET
828
0
92874
TrEMBL
-
A0A0T5Z0G8_9GAMM
845
0
94764
TrEMBL
-
A0A738B8G0_SALET
828
0
92918
TrEMBL
-
A0A3V9E5F6_SALET
828
0
92890
TrEMBL
-
A0A1F6GZD7_9PROT
912
0
100744
TrEMBL
-
A0A1F4QDI9_9BACT
784
0
88207
TrEMBL
-
D4ZL46_SHEVD
Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12)
829
0
93208
TrEMBL
-
A0A4P7TK95_SHIFM
Shigella flexneri serotype 5a (strain M90T)
828
0
92987
TrEMBL
-
M8B5U3_RHIRD
834
0
93435
TrEMBL
-
A0A1J4Z0H6_9PROT
914
0
102498
TrEMBL
-
A0A6L4WWF1_9PROT
934
0
104625
TrEMBL
-
A0A1F7Q1S3_9BACT
784
0
86914
TrEMBL
-
A4Y6P3_SHEPC
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
829
0
92767
TrEMBL
-
A0A7C6Z313_9FIRM
758
0
83739
TrEMBL
-
M4RAT1_BIBTR
827
0
93428
TrEMBL
-
S5JCJ3_VIBPH
829
0
92931
TrEMBL
-
A0A4V3PFI1_9BACT
834
0
93489
TrEMBL
-
A0A5I3WVC1_SALET
828
0
92858
TrEMBL
-
A0A1F7PH87_9BACT
784
0
87316
TrEMBL
-
A0A7C7RBJ6_9BACT
796
0
89070
TrEMBL
-
A0A806DCN1_HAEI6
Haemophilus influenzae (strain R2866)
827
0
93629
TrEMBL
-
A0A656IEE2_SALE2
Salmonella enteritidis (strain 2009K0958)
828
0
92874
TrEMBL
-
A0A8E6IJK9_SALER
828
0
92928
TrEMBL
-
A0A0B4XHT0_9HYPH
835
0
93758
TrEMBL
-
A0A1G3HST6_9RHOO
849
0
95001
TrEMBL
-
A1S9X9_SHEAM
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
827
0
92171
TrEMBL
-
A0A736MDE1_SALHO
828
0
92883
TrEMBL
-
A0A4V1DA19_SALET
828
0
92860
TrEMBL
-
A0A737J0B3_SALER
828
0
92888
TrEMBL
-
A0A736ZDQ0_SALET
828
0
92858
TrEMBL
-
A0A2U8G2G8_RHIFR
834
0
93324
TrEMBL
-
A0A2H0IUX0_9BURK
842
0
93710
TrEMBL
-
A0A369ZQE2_9PAST
827
0
93466
TrEMBL
-
A0A719ZMV7_SALTI
828
0
92858
TrEMBL
-
A0A5I9DQB4_SALET
828
0
92864
TrEMBL
-
A0A6Y5YX81_SALET
828
0
92874
TrEMBL
-
A0A486X9J2_SALET
828
0
92874
TrEMBL
-
A0A1M7T2I4_9FIRM
758
0
83607
TrEMBL
-
A0A0E2L5Q2_ECOU3
Escherichia coli (strain UMEA 3162-1)
828
0
93058
TrEMBL
-
D7A7N0_STAND
Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456)
831
0
92805
TrEMBL
-
A3D3V3_SHEB5
Shewanella baltica (strain OS155 / ATCC BAA-1091)
829
0
92871
TrEMBL
-
A0A8D9JGT7_PSEAI
834
0
93512
TrEMBL
-
A0A8E5IHR1_SALET
828
0
92874
TrEMBL
-
A0A837C307_9BRAD
837
0
94215
TrEMBL
-
A0A447JFD8_SALET
828
0
92904
TrEMBL
-
B8CPC5_SHEPW
Shewanella piezotolerans (strain WP3 / JCM 13877)
829
1
93284
TrEMBL
-
A0A448U101_ACTPL
827
0
93572
TrEMBL
-
A0A4Q0UG27_9PROT
936
0
105841
TrEMBL
-
K8WWV2_9GAMM
828
0
93043
TrEMBL
-
A0A426VXM3_9PROT
945
0
105944
TrEMBL
-
A0A731NBD5_SALER
828
0
92883
TrEMBL
-
A0A2D3W333_9PROT
933
0
105350
TrEMBL
-
A0A7Y8WLH1_9BACI
845
0
95234
TrEMBL
-
A0A5V7D7I0_SALET
828
0
92874
TrEMBL
-
A0A2D3VYW3_9PROT
933
0
105405
TrEMBL
-
A0A7D4T8K9_YERMW
Yersinia mollaretii (strain ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263 / WAIP 204)
831
0
93317
TrEMBL
-
A0A1F9NSI5_9DELT
770
1
86500
TrEMBL
-
A0A7S8AA48_9BRAD
849
0
94971
TrEMBL
-
A0A5I9SCX0_SALET
828
0
92874
TrEMBL
-
A0A1Q3VS99_9PROT
848
0
95058
TrEMBL
-
A0A0A2Y8P7_9PAST
825
0
93022
TrEMBL
-
A0A8E2A9E6_PASMD
828
0
93356
TrEMBL
-
A0A6C7ARE3_SALTU
Salmonella typhimurium (strain ATCC 68169 / UK-1)
828
0
92860
TrEMBL
-
A0A1F2RTV7_9BACT
848
0
93989
TrEMBL
-
A0A497TNL4_9BACT
857
0
96383
TrEMBL
-
B3E655_TRIL1
Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ)
770
0
86488
TrEMBL
-
C9QFI7_VIBOR
829
0
92606
TrEMBL
-
A0A7K0IC94_9ACTN
856
0
94720
TrEMBL
-
A0A2D6CME3_9GAMM
829
0
93619
TrEMBL
-
A0A7Z0VKP1_9GAMM
856
0
95943
TrEMBL
-
A0A3V5ZCA7_SALET
828
0
92874
TrEMBL
-
A0A2R4D7T4_SALET
828
0
92888
TrEMBL
-
A0A5U9QCW4_SALET
828
0
92888
TrEMBL
-
A0A1V3IUA5_9PAST
827
0
93506
TrEMBL
-
A0A5X9XG97_SALET
828
0
92874
TrEMBL
-
O88111_CERSP
831
0
92711
TrEMBL
-
A0A2W5LQM6_9GAMM
830
0
92782
TrEMBL
-
A0A3S7MZN8_9PAST
828
0
93356
TrEMBL
-
A0A1C7HGA0_9BURK
919
0
102403
TrEMBL
-
A0A432EKI7_9GAMM
910
0
102235
TrEMBL
-
A0A7Z0Y7V7_SALDZ
828
0
92912
TrEMBL
-
A0A5I3D336_SALET
828
0
92874
TrEMBL
-
A0A6B2FI15_9ENTR
828
0
92753
TrEMBL
-
A0A2N2VRL4_9PROT
837
0
93482
TrEMBL
-
A0A1F6T7U5_9PROT
848
0
94502
TrEMBL
-
A0A1X9TYP1_PHODD
828
0
93301
TrEMBL
-
A0A085HNQ5_9GAMM
827
0
92626
TrEMBL
-
A0A1V5X862_9DELT
803
0
90444
TrEMBL
-
A0A7K3XZB5_9ACTN
862
0
95474
TrEMBL
-
A0A1G0KZ66_9GAMM
874
0
98777
TrEMBL
-
A0A1V5FCI6_9PROT
848
0
95096
TrEMBL
-
A0A1G1NN20_9BACT
787
0
88494
TrEMBL
-
A0A1G3UFU4_9PROT
939
0
104971
TrEMBL
-
A3QDT8_SHELP
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
831
0
93191
TrEMBL
-
A8H5B0_SHEPA
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
829
0
92905
TrEMBL
-
A0A8E6K5C6_SALET
828
0
92858
TrEMBL
-
A0A741MVU7_SALER
828
0
92847
TrEMBL
-
A0A807ZE14_AERSA
829
1
92835
TrEMBL
-
A0A636NZI6_SALET
828
0
92874
TrEMBL
-
I0GVN9_SELRL
Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421)
757
0
84240
TrEMBL
-
A0A5C1Q4C4_9BURK
849
0
94682
TrEMBL
-
A0A7G9ZCK9_9EURY
111
0
12986
TrEMBL
-
A0A3M1K878_9BACT
770
0
86938
TrEMBL
-
A0A603BI86_SALER
828
0
92874
TrEMBL
-
A0A1F7M2B1_9BACT
784
0
87245
TrEMBL
-
A0A8F7R448_SALER
828
0
92814
TrEMBL
-
A0A649PT43_CAMJU
924
0
104926
TrEMBL
-
A0A2M7D1G8_9GAMM
831
0
92359
TrEMBL
-
A0A740VFM8_SALET
828
0
92847
TrEMBL
-
A0A5H6AJ25_SALET
828
0
92874
TrEMBL
-
A0A2M8B0C0_9DELT
923
0
104111
TrEMBL
-
A0A661I159_9PROT
937
0
105291
TrEMBL
-
A0A3N9QE81_9RHOB
833
0
93632
TrEMBL
-
A0A222MWM8_9PROT
924
0
105006
TrEMBL
-
A0A1S0ZNM4_SALET
828
0
92874
TrEMBL
-
A0A5H8JUX2_SALET
828
0
92874
TrEMBL
-
A0A4Z8Y5L3_SALET
828
0
92874
TrEMBL
-
A0A725BET9_SALEP
Salmonella enteritidis PT4 (strain P125109)
828
0
92874
TrEMBL
-
A0A730CAC2_SALET
828
0
92874
TrEMBL
-
A0A4Y6N1L6_SALET
828
0
92858
TrEMBL
-
A0A494T2K5_9PROT
936
0
105737
TrEMBL
-
A0A1E4K9I3_9GAMM
830
0
92751
TrEMBL
-
A0A5X8YXF9_SALET
828
0
92864
TrEMBL
-
I2B9N6_SHIBC
Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74)
828
0
92676
TrEMBL
-
A0A1G0LHV8_9DELT
775
0
86699
TrEMBL
-
A0A7X2KDM3_9PROT
832
0
93409
TrEMBL
-
A0A3R1BSB8_SALET
828
0
92874
TrEMBL
-
A0A011NM01_9PROT
841
0
94149
TrEMBL
-
A0A718YHS6_SALTS
Salmonella typhimurium (strain SL1344)
828
0
92890
TrEMBL
-
B8CTJ1_SHEPW
Shewanella piezotolerans (strain WP3 / JCM 13877)
827
0
92322
TrEMBL
-
M1PR19_DESSD
Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1)
795
0
89101
TrEMBL
-
A0A2S5J738_CAMHY
926
0
104452
TrEMBL
-
A0A2M7I8Q7_9PROT
914
0
102498
TrEMBL
-
A0A1F6V2U9_9PROT
830
0
93040
TrEMBL
-
A0A2N1XDF7_9GAMM
830
0
92485
TrEMBL
-
V6F186_MAGGM
Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
835
0
93629
TrEMBL
-
A0A3S5YGD0_SALER
828
0
92847
TrEMBL
-
A0A1S7RUZ4_9HYPH
Agrobacterium tomkonis CFBP 6623
834
0
93482
TrEMBL
-
A4WZN0_CERS5
Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
831
0
92796
TrEMBL
-
A4WXJ2_CERS5
Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
828
0
92595
TrEMBL
-
A0A1T4PMC8_9FIRM
749
0
83940
TrEMBL
-
A0A2T3L0L8_PHOLD
828
0
93244
TrEMBL
-
A0A1V3TJQ2_9PAST
826
0
93094
TrEMBL
-
A0A8E6KNP1_SALET
828
0
92874
TrEMBL
-
A0A562DIK9_9GAMM
831
0
92851
TrEMBL
-
A0A656HEG8_THINJ
Thiothrix nivea (strain ATCC 35100 / DSM 5205 / JP2)
859
0
96757
TrEMBL
-
A0A5J0I295_SALET
828
0
92888
TrEMBL
-
A0A1G0AUL5_9PROT
909
0
101642
TrEMBL
-
A0A5I5E247_SALET
828
0
92874
TrEMBL
-
A0A0S8DTU0_9GAMM
834
0
93727
TrEMBL
-
A0A729K9J8_SALHO
828
0
92883
TrEMBL
-
A0A496XVH6_9PROT
948
0
107126
TrEMBL
-
A0A645IN25_9ZZZZ
102
0
11361
TrEMBL
other Location (Reliability: 2)
A0A2K2HAK4_9DELT
773
0
86526
TrEMBL
-
A0A5I1Z7M4_SALET
828
0
92894
TrEMBL
-
A0A5I1S085_SALET
828
0
92874
TrEMBL
-
A0A3Y3TLZ7_SALER
828
0
92874
TrEMBL
-
A0A5I1MJ28_SALET
828
0
92874
TrEMBL
-
G8QFB2_AZOOP
Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS)
841
0
94036
TrEMBL
-
A0A826DZT0_CAMJU
924
0
104944
TrEMBL
-
A0A2W5LQC5_9GAMM
832
0
92998
TrEMBL
-
A0A8B6KUH6_YEREN
831
0
93407
TrEMBL
-
A0A658A9K2_ALCXX
831
0
93142
TrEMBL
-
A0A2N2S0R3_9PROT
837
0
93097
TrEMBL
-
A0A2U8FIJ3_9PAST
835
0
94540
TrEMBL
-
A0A140N7W5_ECOBD
Escherichia coli (strain B / BL21-DE3)
828
0
93060
TrEMBL
-
I3X957_SINF2
Sinorhizobium fredii (strain USDA 257)
834
0
93339
TrEMBL
-
A0A2N3EQC0_9PROT
830
0
92749
TrEMBL
-
A0A1E7J9M7_9DELT
772
0
87026
TrEMBL
-
A0A806G5W9_AGGAC
828
0
93492
TrEMBL
-
A0A5I4KIF6_SALET
828
0
92864
TrEMBL
-
A0A1F9M2L2_9DELT
772
0
85667
TrEMBL
-
A0A701VXK9_SALER
828
0
92888
TrEMBL
-
A0A0C5WD26_9GAMM
828
0
93163
TrEMBL
-
A0A023XQ02_BRAJP
837
0
94153
TrEMBL
-
H2FWI6_OCESG
Oceanimonas sp. (strain GK1 / IBRC-M 10197)
829
0
93201
TrEMBL
-
A0A6I3SC05_9BURK
921
0
103172
TrEMBL
-
A0A1F3ZQY1_9PROT
840
0
93581
TrEMBL
-
A0A5X3NZQ5_SALET
828
0
92830
TrEMBL
-
A0A562RWV5_9BRAD
837
0
94229
TrEMBL
-
A0A8E9YQT9_SALET
828
0
92874
TrEMBL
-
A4YA77_SHEPC
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
826
0
92335
TrEMBL
-
A0A2T9ZR85_9GAMM
856
0
95832
TrEMBL
-
A0A6N4CZD9_AERSA
829
1
92835
TrEMBL
-
A0A379XN09_SALER
828
0
92897
TrEMBL
-
A0A1H7ZQ61_9FIRM
750
0
83577
TrEMBL
-
A8H064_SHEPA
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
826
0
92363
TrEMBL
-
A0A381DL97_9PROT
928
0
104740
TrEMBL
-
I9NDF4_RHILT
835
0
93353
TrEMBL
-
A0A729G872_SALHO
828
0
92883
TrEMBL
-
A0A2M8BJ63_9BURK
840
1
93907
TrEMBL
-
F2KF42_PSEBN
Pseudomonas brassicacearum (strain NFM421)
834
0
93648
TrEMBL
-
A0A7U7G1Y4_YEREN
831
0
93416
TrEMBL
-
A0A7C2DDF2_9BACT
792
0
89471
TrEMBL
-
A0A1J6Z417_SALHO
828
0
92883
TrEMBL
-
Q24Q25_DESHY
Desulfitobacterium hafniense (strain Y51)
758
0
83445
TrEMBL
-
A0A0A6NZT6_9GAMM
835
0
94472
TrEMBL
-
A0A0S4HQM7_9PSED
834
0
94123
TrEMBL
-
A0A248K8N8_SALBN
828
0
93011
TrEMBL
-
A0A5H6P1U3_SALET
828
0
92890
TrEMBL
-
A0A702FDQ4_SALET
828
0
92874
TrEMBL
-
A0A2I8S8N4_9ENTR
828
0
92954
TrEMBL
-
A0A1F6LTM4_9BACT
743
0
83860
TrEMBL
-
A0A1H1JFC8_9HYPH
832
0
93120
TrEMBL
-
A0A0S8AKM1_9BACT
922
0
104304
TrEMBL
-
A0A3T3G9Q5_SALET
828
0
92874
TrEMBL
-
A0A0D6HB42_ALCXX
831
0
93413
TrEMBL
-
A0A3T2YS01_SALET
828
0
92874
TrEMBL
-
A0A701UFW0_SALHO
828
0
92883
TrEMBL
-
A0A659NCK4_SALET
828
0
92874
TrEMBL
-
A0A3T2WJ62_SALET
828
0
92874
TrEMBL
-
A0A5I1I002_SALET
828
0
92874
TrEMBL
-
A0A1E5BX56_9GAMM
828
0
92145
TrEMBL
-
C7RM78_ACCPU
Accumulibacter phosphatis (strain UW-1)
841
0
94032
TrEMBL
-
A0A8D3XZW7_9PSED
834
0
93380
TrEMBL
-
A0A2N1ZFL8_9GAMM
834
0
93578
TrEMBL
-
A0A1J0LNZ3_9FLAO
781
0
87500
TrEMBL
-
I7H567_9HELI
937
0
105412
TrEMBL
-
A0A734HN11_SALER
828
0
92883
TrEMBL
-
A0L807_MAGMM
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
837
0
94149
TrEMBL
-
A0A7Y2EB82_9BACT
782
0
87148
TrEMBL
-
A0A718HRR7_SALTS
Salmonella typhimurium (strain SL1344)
828
0
92860
TrEMBL
-
A0A6M3NWB3_SALET
828
0
92860
TrEMBL
-
A0A6Y0YNG2_SALET
828
0
92821
TrEMBL
-
A0A7U7IML9_YEREN
831
0
93416
TrEMBL
-
A0A2G1DK19_9PROT
933
0
105537
TrEMBL
-
A0A516WD36_9BURK
846
0
94704
TrEMBL
-
F8E848_FLESM
Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10)
797
0
89244
TrEMBL
-
B6IR10_RHOCS
Rhodospirillum centenum (strain ATCC 51521 / SW)
841
0
94445
TrEMBL
-
E1SPK4_FERBD
Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT)
826
0
91800
TrEMBL
-
A0A2T6MWJ0_9GAMM
856
0
95753
TrEMBL
-
A0A2H1E9N3_9FLAO
775
0
87112
TrEMBL
-
A0A7W7Z5J1_9BRAD
837
0
93598
TrEMBL
-
A0A080IY53_ECOLX
828
0
93038
TrEMBL
-
A0A5C4QHJ2_9PAST
826
0
93245
TrEMBL
-
A0A256W7P6_9BACT
929
0
104670
TrEMBL
-
A0A1E5CMX2_9VIBR
829
0
92750
TrEMBL
-
A0A0F2RME6_9PROT
828
1
92177
TrEMBL
-
A0A5W2AA88_SALET
828
0
92874
TrEMBL
-
A0A702P992_SALER
828
0
92902
TrEMBL
-
A0A6I2JFG2_9ENTR
828
0
92474
TrEMBL
-
G0L7E1_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
775
0
86892
TrEMBL
-
A0A5H7D2V1_SALET
828
0
92874
TrEMBL
-
A0A644T717_9ZZZZ
936
0
105653
TrEMBL
Mitochondrion (Reliability: 5)
A0A644T3J2_9ZZZZ
756
1
83522
TrEMBL
Mitochondrion (Reliability: 5)
A0A5W1EEN5_SALER
828
0
92847
TrEMBL
-
A0A3V4QFV6_SALET
828
0
92874
TrEMBL
-
A0A4U8J919_SALET
828
0
92888
TrEMBL
-
A0A0B4Y1T8_9PROT
834
0
94082
TrEMBL
-
A0A2S3VPG5_9PSED
834
0
93946
TrEMBL
-
A0A5J0F9J2_SALET
828
0
92864
TrEMBL
-
A0A0H3EJA5_ECO8N
Escherichia coli O83:H1 (strain NRG 857C / AIEC)
828
0
93070
TrEMBL
-
A0A8E6JA81_SALNE
828
0
92874
TrEMBL
-
F3QI87_9BURK
921
0
103158
TrEMBL
-
A0A7G9YEJ7_9EURY
433
0
47422
TrEMBL
-
A0A1E7JCK9_9DELT
798
0
89866
TrEMBL
-
A0A258TN75_9PROT
914
0
102512
TrEMBL
-
E5YHC2_9ENTR
830
0
92864
TrEMBL
-
A0A0E1GIZ6_CAMFE
925
0
104255
TrEMBL
-
A0A2H0G2H6_9PROT
841
0
93947
TrEMBL
-
A0A1F7M2A4_9BACT
784
0
87340
TrEMBL
-
A0A1S6U6A6_9PROT
925
0
104455
TrEMBL
-
A0A1B3JH94_9PAST
827
0
93471
TrEMBL
-
U2Z0I7_PSEA4
Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 / NCTC 10367 / 1577)
834
0
93178
TrEMBL
-
A0A5I9BFS8_SALET
828
0
92874
TrEMBL
-
A0A4U7BJ99_9PROT
925
0
104276
TrEMBL
-
A0A737LJX4_SALER
828
0
92883
TrEMBL
-
A0A254TCC2_9BURK
831
0
93424
TrEMBL
-
D1B0Y8_SULD5
Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175)
929
0
104420
TrEMBL
-
A0A2I8TNN4_9ENTR
828
0
93090
TrEMBL
-
H0KGJ9_AGGAC
828
0
93405
TrEMBL
-
A0A345J2M2_9PROT
938
0
105709
TrEMBL
-
A0A370D962_9GAMM
845
0
95331
TrEMBL
-
A0A1B7I3Q1_9ENTR
828
0
92521
TrEMBL
-
A0A6N8IL06_9ACTN
856
0
94721
TrEMBL
-
A0A4V3D9G8_9PAST
826
0
92994
TrEMBL
-
A0A2N1Y4V7_9GAMM
831
1
92675
TrEMBL
-
A0A1S7R364_RHIRD
834
0
93385
TrEMBL
-
C6WXA3_METML
Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540)
905
0
99502
TrEMBL
-
Q2IPE7_ANADE
Anaeromyxobacter dehalogenans (strain 2CP-C)
752
0
82305
TrEMBL
-
NAPB_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
169
0
18924
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
17000
90000
16000
P33937; P0ABL3
1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE
16000
-
x * 90000 + x * 16000, two-subunit complex, NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster. NapB is an 16000 Da electron-transfer subunit, which in other bacteria binds two c-type haems
17000
-
1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively
90000
-
1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively
90000
P33937; P0ABL3
1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE
90000
-
x * 90000 + x * 16000, two-subunit complex, NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster. NapB is an 16000 Da electron-transfer subunit, which in other bacteria binds two c-type haems
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
additional information
?
-
x * 90000 + x * 16000, two-subunit complex, NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster. NapB is an 16000 Da electron-transfer subunit, which in other bacteria binds two c-type haems
?
-
1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively
heterodimer
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
1 * 17000 + 1 * 87000, SDS-PAGE
-
heterodimer
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
1 * 93309 + 1 * 18924, calculated from sequence
-
heterodimer
P33937; P0ABL3
1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
-
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
-
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
PELDOR analysis of recombinant MTSL-labelled MalE-NapASP fusion mutant S4C/S24C alone or in complex with NapD, comparison of bound, NMR-derived NapASP helix from PDB ID 2PQ4 versus free generated helix, positions of the spin labels in the two conformations of the signal peptide, overview
additional information
-
PELDOR analysis of recombinant MTSL-labelled MalE-NapASP fusion mutant S4C/S24C alone or in complex with NapD, comparison of bound, NMR-derived NapASP helix from PDB ID 2PQ4 versus free generated helix, positions of the spin labels in the two conformations of the signal peptide, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the nap operon of Escherichia coli K-12, encoding a periplasmic nitrate reductase, encodes seven proteins. The catalytic complex in the periplasm, NapANapB receives electrons from the quinol pool via the membrane-bound cytochrome NapC. Like NapA, B and C, NapD, is also essential for Nap activity. None of the remaining three polypeptides, NapF, G and H, which are predicted to encode non-heme, iron-sulfur proteins, are essential for Nap activity
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
-
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
-
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
P33937; P0ABL3
the pre-NapA leader sequence is both unexpectedly long and, unless two successive proteolysis steps are involved, is cleaved at the unprecedented sequence G-Q-Q
additional information
-
NapF plays a role in the post-translational modification of NapA prior to the export of folded NapA via the twin-arginine translocation pathway into the periplasm
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure, the substrate channel and catalytic pocket are more basic than other NapA proteins, which may influence the substrate binding as well as product release
sitting-drop vapour-diffusion method, crystals of the oxidized form of this enzyme are obtained using polyethylene glycol 3350 as precipitant. A single crystal diffracted to beyond 1.5 A at the ESRF (ID14-1), which is the highest resolution reported to date for a nitrate reductase. The unit-cell parameters are a = 142.2, b = 82.4, c = 96.8 A, beta = 100.7°, space group C2, and one heterodimer is present per asymmetric unit
-
X-ray diffraction structure analysis, resolution 2.2 A, PDB ID 2jio, modelling
purified recombinant NapDNHis/NapA complex, small angle X-ray scattering analysis, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C176S
S4C/S24C
site-directed mutagenesis, native, NapD results in a loss of some of the spin labels from the NapA signal peptide possibly due to the surface-exposed native cysteine residues of NapD. The NapD cysteine residues (C8 and C32) are not conserved and a cysteine-free variant of NapD complements a DELTAnapD strain for restoration of NapA activity. A NapD C8S/C32A variant remains attached to the NapA signal peptide
additional information
C176S
mutation in strictly conserved residue, significantly lower activity than wild-type
C176S
-
mutation in strictly conserved residue, significantly lower activity than wild-type
-
additional information
genotyping of different strains from M and G populations, overview. The only mutated gene shared between the strains from populations M and G is bll4572, this gene encodes the Bll4572 protein and is mutated in all six strains. Regulation of nos and nap genes by the NasST system in the absence or presence of nitrate in mutant strains, overview. NasS and NasT form a stable complex that is sensitive to the presence of NO3-/NO2-. Binding of NO3-/NO2- by the sensor NasS triggers the release of NasT, which binds the leader sequence upstream of the nas operon, thereby preventing hairpin formation and allowing complete transcription of the nas operon
additional information
-
genotyping of different strains from M and G populations, overview. The only mutated gene shared between the strains from populations M and G is bll4572, this gene encodes the Bll4572 protein and is mutated in all six strains. Regulation of nos and nap genes by the NasST system in the absence or presence of nitrate in mutant strains, overview. NasS and NasT form a stable complex that is sensitive to the presence of NO3-/NO2-. Binding of NO3-/NO2- by the sensor NasS triggers the release of NasT, which binds the leader sequence upstream of the nas operon, thereby preventing hairpin formation and allowing complete transcription of the nas operon
additional information
Bradyrhizobium japonicum JCM 10833
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genotyping of different strains from M and G populations, overview. The only mutated gene shared between the strains from populations M and G is bll4572, this gene encodes the Bll4572 protein and is mutated in all six strains. Regulation of nos and nap genes by the NasST system in the absence or presence of nitrate in mutant strains, overview. NasS and NasT form a stable complex that is sensitive to the presence of NO3-/NO2-. Binding of NO3-/NO2- by the sensor NasS triggers the release of NasT, which binds the leader sequence upstream of the nas operon, thereby preventing hairpin formation and allowing complete transcription of the nas operon
-
additional information
-
the physiological role of NAP in nitrate metabolism is investigated in studies with a mutant bearing a transposon insertion in one of the structural genes
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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the physiological role of NAP in nitrate metabolism is investigated in studies with a mutant bearing a transposon insertion in one of the structural genes
-
additional information
construction of a gene nap deletion mutant, the wild-type gene is replaced by the deletion/insertion version via homologous recombination. The mutant strain can no longer grow on methanol in contrast to the wild-type
additional information
-
construction of a gene nap deletion mutant, the wild-type gene is replaced by the deletion/insertion version via homologous recombination. The mutant strain can no longer grow on methanol in contrast to the wild-type
-
additional information
-
constructin of a napA mutant strain CAL277, and of several other nap gene mutants, overview
additional information
-
constructin of a napA mutant strain CAL277, and of several other nap gene mutants, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, about 90% of the activity is lost after 48 h, no activity remains after 4 days
P33937; P0ABL3
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of recombinant NapA complexed with N-terminally His-tagged NapD activator by nickel afinity chromatography from Escherichia coli strains MC4100 and BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene napA, enzyme NapA is encoded, along with its periplasmic di-heme c-type cytochrome redox partner NapB, in the seven gene nap operon, coexpression of NapA with His-tagged NapD activator in Escherichia coli strains MC4100 and BL21(DE3), recombinant expression of MTSL-labelled MalE-NapASP fusion mutant S4C/S24C in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain LCB2048
structural genes, napA and napB, are cloned, and their nucleotide sequences is determined
-
gene nap and nap gene cluster, genetic organization and sequence comparisons
-
gene nap and nap gene cluster, genetic organization and sequence comparisons
-
gene nap and nap gene cluster, genetic organization and sequence comparisons
-
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
gene nap and nap gene cluster, genetic organization and sequence comparisons
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
disruption of nasT leads to a marked decrease in nosZ and nap transcription in cells incubated in the presence of nitrate
in the absence of nitrate, mutated nasS, which encodes the nitrate (NO3-)-sensor of the two-component NasST regulatory system, induces expression of nosZ and periplasmic nitrate reductase nap via nasT. Nitrate addition dissociates the NasS-NasT complex in vitro, suggesting the release of the activator NasT
NarL represses the expression of periplasmic nitrate reductase NapAB under anaerobiosis
-
disruption of nasT leads to a marked decrease in nosZ and nap transcription in cells incubated in the presence of nitrate
disruption of nasT leads to a marked decrease in nosZ and nap transcription in cells incubated in the presence of nitrate
Bradyrhizobium japonicum JCM 10833
-
-
in the absence of nitrate, mutated nasS, which encodes the nitrate (NO3-)-sensor of the two-component NasST regulatory system, induces expression of nosZ and periplasmic nitrate reductase nap via nasT. Nitrate addition dissociates the NasS-NasT complex in vitro, suggesting the release of the activator NasT
in the absence of nitrate, mutated nasS, which encodes the nitrate (NO3-)-sensor of the two-component NasST regulatory system, induces expression of nosZ and periplasmic nitrate reductase nap via nasT. Nitrate addition dissociates the NasS-NasT complex in vitro, suggesting the release of the activator NasT
Bradyrhizobium japonicum JCM 10833
-
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
immobilization of whole cells and NAP enzyme for simultaneous bioremediation and bionanoparticles synthesis. The immobilized cells completely remove NO3- upon 192 h with Ag nanoparticles synthesis ranging from 23.26 to 58.14 nm. Immobilized NAP exhibits lower efficiency with 28.6% of NO3- elimination within 288 h and large aggregated Ag nanoparticles ranging from 94.44 nm to 172.22 nm
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Pittman, M.S.; Kelly, D.J.
Electron transport through nitrate and nitrite reductases in Campylobacter jejuni
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Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli
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282
6425-6437
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Escherichia coli
Nilavongse, A.; Brondijk, T.H.; Overton, T.W.; Richardson, D.J.; Leach, E.R.; Cole, J.A.
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Microbiology
152
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2006
Escherichia coli
Gates, A.J.; Richardson, D.J.; Butt, J.N.
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409
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63
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Cupriavidus necator H16
Brondijk, T.H.; Nilavongse, A.; Filenko, N.; Richardson, D.J.; Cole, J.A.
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379
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Escherichia coli K-12
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Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions.
Biochim. Biophys. Acta
1232
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1995
Cupriavidus necator, Escherichia coli, Paracoccus denitrificans, Paracoccus pantotrophus
Durvasula, K.; Jantama, K.; Fischer, K.; Vega, A.; Koopman, B.; Svoronos, S.A.
Effect of periplasmic nitrate reductase on diauxic lag of Paracoccus pantotrophus
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25
973-979
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Paracoccus pantotrophus (Q56350), Paracoccus pantotrophus
Berks, B.C.; Richardson, D.J.; Robinson, C.; Reilly, A.; Aplin, R.T.; Ferguson, S.J.
Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha
Eur. J. Biochem.
220
117-124
1994
Paracoccus pantotrophus
Sears, H.J.; Ferguson, S.J.; Richardson, D.J.; Spiro, S.
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113
107-112
1993
Paracoccus denitrificans
-
Thomas, G.; Potter, L.; Cole, J.A.
The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site
FEMS Microbiol. Lett.
174
167-171
1999
Escherichia coli K-12 (P33937 and P0ABL3)
Siddiqui, R.A.; Warnecke-Eberz, U.; Hengsberger, A.; Schneider, B.; Kostka, S.; Friedrich, B.
Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16
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175
5867-5876
1993
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Wang, H.; Tseng, C.P.; Gunsalus, R.P.
The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite
J. Bacteriol.
181
5303-5308
1999
Escherichia coli
Stewart, V.; Bledsoe, P.J.; Chen, L.L.; Cai, A.
Catabolite repression control of napF (periplasmic nitrate reductase) operon expression in Escherichia coli K-12
J. Bacteriol.
191
996-1005
2009
Paracoccus pantotrophus
Hofmann, M.
Density functional theory study of model complexes for the revised nitrate reductase active site in Desulfovibrio desulfuricans NapA
J. Biol. Inorg. Chem.
14
1023-1035
2009
Desulfovibrio desulfuricans
Cerqueira, N.M.; Gonzalez, P.J.; Brondino, C.D.; Romao, M.J.; Romao, C.C.; Moura, I.; Moura, J.J.
The effect of the sixth sulfur ligand in the catalytic mechanism of periplasmic nitrate reductase
J. Comput. Chem.
30
2466-2484
2009
Desulfovibrio desulfuricans
Brondijk, T.H.; Fiegen, D.; Richardson, D.J.; Cole, J.A.
Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation
Mol. Microbiol.
44
245-255
2002
Escherichia coli K-12
Van Alst, N.E.; Sherrill, L.A.; Iglewski, B.H.; Haidaris, C.G.
Compensatory periplasmic nitrate reductase activity supports anaerobic growth of Pseudomonas aeruginosa PAO1 in the absence of membrane nitrate reductase
Can. J. Microbiol.
55
1133-1144
2009
Pseudomonas aeruginosa
Simpson, P.J.; Richardson, D.J.; Codd, R.
The periplasmic nitrate reductase in Shewanella: the resolution, distribution and functional implications of two NAP isoforms, NapEDABC and NapDAGHB
Microbiology
156
302-312
2010
Shewanella amazonensis, Shewanella amazonensis SB2B, Shewanella baltica, Shewanella baltica OS155, Shewanella baltica OS185, Shewanella baltica OS195, Shewanella baltica OS223, Shewanella denitrificans, Shewanella denitrificans OS217, Shewanella frigidimarina, Shewanella halifaxensis, Shewanella loihica, Shewanella loihica PV-4, Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550, Shewanella pealeana, Shewanella piezotolerans, Shewanella piezotolerans WP3, Shewanella putrefaciens, Shewanella putrefaciens CN-32, Shewanella sediminis, Shewanella sp., Shewanella sp. ANA-3, Shewanella sp. MR-4, Shewanella sp. MR-7, Shewanella sp. W3-18-1, Shewanella woodyi
Cerqueira, N.M.; Gonzalez, P.J.; Fernandes, P.A.; Moura, J.J.; Ramos, M.J.
Periplasmic nitrate reductase and formate dehydrogenase similar molecular architectures with very different enzymatic activities
Acc. Chem. Res.
48
2875-2884
2015
Methylotenera mobilis (C6WXA3), Desulfovibrio desulfuricans (P81186), Methylotenera mobilis JLW8 (C6WXA3)
Jacques, J.G.; Burlat, B.; Arnoux, P.; Sabaty, M.; Guigliarelli, B.; Leger, C.; Pignol, D.; Fourmond, V.
Kinetics of substrate inhibition of periplasmic nitrate reductase
Biochim. Biophys. Acta
1837
1801-1809
2014
Cereibacter sphaeroides (Q53176), Cereibacter sphaeroides DSM 158 (Q53176)
Gonzalez, P.; Rivas, M.; Mota, C.; Brondino, C.; Moura, I.; Moura, J.
Periplasmic nitrate reductases and formate dehydrogenases biological control of the chemical properties of Mo and W for fine tuning of reactivity, substrate specificity and metabolic role
Coord. Chem. Rev.
257
315-331
2013
Anaeromyxobacter dehalogenans (Q2IPE7), Bradyrhizobium japonicum, Campylobacter jejuni subsp. jejuni (Q9PPD9), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q9PPD9), Cereibacter sphaeroides (Q53176), Cupriavidus necator (P39185), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (P39185), Desulfitobacterium hafniense (A0A098B5Y5), Desulfovibrio desulfuricans (P81186), Escherichia coli (P33937), Paracoccus denitrificans (A1BB88), Paracoccus pantotrophus (Q56350), Paracoccus pantotrophus GB17 (Q56350), Pseudomonas sp. (Q9RC05), Pseudomonas sp. G-179 (Q9RC05), Shewanella gelidimarina (E2F391), Shewanella oneidensis, Wolinella succinogenes
-
Sanchez, C.; Itakura, M.; Okubo, T.; Matsumoto, T.; Yoshikawa, H.; Gotoh, A.; Hidaka, M.; Uchida, T.; Minamisawa, K.
The nitrate-sensing NasST system regulates nitrous oxide reductase and periplasmic nitrate reductase in Bradyrhizobium japonicum
Environ. Microbiol.
16
3263-3274
2014
Bradyrhizobium japonicum (Q89EN5), Bradyrhizobium japonicum, Bradyrhizobium japonicum JCM 10833 (Q89EN5)
Dow, J.M.; Grahl, S.; Ward, R.; Evans, R.; Byron, O.; Norman, D.G.; Palmer, T.; Sargent, F.
Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone
FEBS J.
281
246-260
2014
Escherichia coli (P33937), Escherichia coli
Lopez, C.A.; Rivera-Chavez, F.; Byndloss, M.X.; Baeumler, A.J.
The periplasmic nitrate reductase NapABC supports luminal growth of Salmonella enterica serovar typhimurium during colitis
Infect. Immun.
83
3470-3478
2015
Salmonella enterica, Salmonella enterica SL1344 AND CAL128
Cerqueira, N.M.; Fernandes, P.A.; Gonzalez, P.J.; Moura, J.J.; Ramos, M.J.
The sulfur shift an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase
Inorg. Chem.
52
10766-10772
2013
Desulfovibrio desulfuricans (P81186)
Zeamari, K.; Gerbaud, G.; Grosse, S.; Fourmond, V.; Chaspoul, F.; Biaso, F.; Arnoux, P.; Sabaty, M.; Pignol, D.; Guigliarelli, B.; Burlat, B.
Tuning the redox properties of a [4Fe-4S] center to modulate the activity of Mo-bisPGD periplasmic nitrate reductase
Biochim. Biophys. Acta Bioenerg.
1860
402-413
2019
Cereibacter sphaeroides f. sp. denitrificans (O88111 and O88160)
Eltarahony, M.; Zaki, S.; Kheiralla, Z.; Abd-El-Haleem, D.
NAP enzyme recruitment in simultaneous bioremediation and nanoparticles synthesis
Biotechnol. Rep.
18
e00257
2018
Achromobacter sp. MMT
Lecomte, S.; Nesme, X.; Franzino, T.; Villard, C.; Pivard, M.; Vial, L.; Dore, J.; Hommais, F.; Haichar, F.
Agrobacterium fabrum C58 involved nitrate reductase NapA and antisense RNA NorR to denitrify
FEMS Microbiol. Ecol.
97
fiaa233
2021
Agrobacterium fabrum (Q8U7P1), Agrobacterium fabrum, Agrobacterium fabrum C58 (Q8U7P1), Agrobacterium fabrum C58
Mintmier, B.; McGarry, J.M.; Sparacino-Watkins, C.E.; Sallmen, J.; Fischer-Schrader, K.; Magalon, A.; McCormick, J.R.; Stolz, J.F.; Schwarz, G.; Bain, D.J.; Basu, P.
Molecular cloning, expression and biochemical characterization of periplasmic nitrate reductase from Campylobacter jejuni
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365
fny151
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Campylobacter jejuni (Q5HV12), Campylobacter jejuni, Campylobacter jejuni RM1221 (Q5HV12)
Siqueira, A.; Sugawara, M.; Arashida, H.; Minamisawa, K.; Sanchez, C.
Levels of periplasmic nitrate reductase during denitrification are lower in Bradyrhizobium japonicum than in Bradyrhizobium diazoefficiens
Microbes Environ.
35
1-5
2020
Bradyrhizobium diazoefficiens (Q89EN5), Bradyrhizobium diazoefficiens, Bradyrhizobium diazoefficiens USDA 110 (Q89EN5), Bradyrhizobium japonicum (Q8KY07), Bradyrhizobium japonicum
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Transporter Classification Database (TCDB): 3.D.11.1.1
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