Information on EC 1.97.1.9 - selenate reductase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
1.97.1.9
-
RECOMMENDED NAME
GeneOntology No.
selenate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors
-
-
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
electron transport mechanism
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
active site molybdenum
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
selenate transport mechanism
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
active site molybdenum
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Selenocompound metabolism
-
SYSTEMATIC NAME
IUBMB Comments
selenite:reduced acceptor oxidoreductase
The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma) that contains molybdenum, iron, acid-labile sulfide and heme b as cofactor constituents. Nitrate, nitrite, chlorate and sulfate are not substrates. A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
selenate reductase
-
-
selenate reductase
Enterobacter cloacae SLD1a-1
-
;
-
selenate reductase
-
-
selenate reductase
-
-
selenate reductase
-
-
-
selenate reductase
-
-
additional information
-
enzyme probably belongs to the DMSO reductase family of mononuclear molybdenum enzymes
additional information
-
enzyme probably belongs to the DMSO reductase family of mononuclear molybdenum enzymes
-
CAS REGISTRY NUMBER
COMMENTARY
146359-71-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ATCC 700258
-
-
Manually annotated by BRENDA team
strain SLD1a-1
-
-
Manually annotated by BRENDA team
strain SLD1a-1, expression under aerobic conditions, poor expression during anaerobic growth on nitrate
-
-
Manually annotated by BRENDA team
strain SLD1a-1; strain SLD1a-1, ATCC 700258, highest activity when molybdate is added to the culture medium
-
-
Manually annotated by BRENDA team
strain SLDa-1
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
-
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
ATCC 700258
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
strain SLD1a-1
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
strain SLD1a-1, expression under aerobic conditions, poor expression during anaerobic growth on nitrate
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
strain SLD1a-1; strain SLD1a-1, ATCC 700258, highest activity when molybdate is added to the culture medium
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLDa-1
strain SLDa-1
-
-
Manually annotated by BRENDA team
genes ygfK, ygfM, and ygfN encode the 3 subunit polypeptides YgfK, YgfM, and YgfN; strain K-12 and derivatives
-
-
Manually annotated by BRENDA team
strain CA5
-
-
Manually annotated by BRENDA team
strain CA5
-
-
Manually annotated by BRENDA team
-
Q9S1H0 and Q9S1G9 and Q9S1G7
UniProt
Manually annotated by BRENDA team
selenate-respiring bacterium
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
selenate + acetate
selenite + H2O + CO2
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
specific for selenate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
specific for selenate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
enzyme also reduces nitrate, thiosulfate, and fumarate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
enzyme also reduces nitrate, thiosulfate, and fumarate, selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized donor
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + glucose
?
show the reaction diagram
-
-
-
-
?
selenate + H2
selenite + H2O
show the reaction diagram
-
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
-
-
-
?
selenate + malate
?
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
detoxification of selenate
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae SLDa-1
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
-
best electron donor
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + benzyl viologen
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + reduced cytc-Ts4
selenite + H2O + oxidized cytc-Ts4
show the reaction diagram
-
a c-type cytochrom is purified and shown to donate electrons to SerABC in vitro. Redox potentiometry, combined with UV-visible spectroscopy, show that cytc-Ts4 is a diheme cytochrome with a redox potential of +/-282 mV, and both hemes are predicted to have His-Met ligation
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
preferred electron donor
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
11% of the activity with benzyl viologen
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
preferred electron donor
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + methyl viologen
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
NADH, succinate, and lactate are no electron donors, no activity with nitrate, nitrite, sulfate, and chlorate
-
-
-
additional information
?
-
-
no activity with nitrate, nitrite, sulfate, and chlorate
-
-
-
additional information
?
-
-
also active on nitrate, thiosulfate and fumarate
-
-
-
additional information
?
-
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
no substrate: nitrate, sulfate, perchlorate, thiosulfate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + H2
selenite + H2O
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
detoxification of selenate
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae SLDa-1
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cytochrome b
-
1 cytochrome b per alphabetagamma-trimer
-
cytochrome b
-
-
-
cytochrome b
-
-
-
heme
-
0.9 mol per mol of enzyme
iron-sulfur centre
-
at least 2 [Fe-S]-centre as prosthetic groups per enzyme molecule
molybdopterin
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Iron
-
12.9 mol per mol of enzyme, based on MW 159000; part of at least 2 iron-sulfur centres per enzyme molecule and of the heme group of cytochrome b
Iron
-
in FeS-centres
Iron
-
iron-sulfur centre
Iron
-
non-heme iron, 18 mol per mol of enzyme
Iron
-
[3Fe4S]1+ and [4Fe4S]1+ centres
Molybdenum
-
1 molybdenum per mol of trimer
Molybdenum
-
in the active site
Molybdenum
-
-
Molybdenum
-
enhances the activity 10fold in vivo when added to the growth medium; required
Molybdenum
-
present at the active site
Molybdenum
-
Mo-S, Mo=O and Mo-O bound to enzyme
Molybdenum
-
0.6 mol per mol of enzyme
Molybdenum
-
type II molybdoenzyme
Molybdenum
-
-
Non-heme iron
-
-
selenium
-
isolated enzyme contains a reduced form of selenium, probably as selenocysteine
sulfur
-
iron-sulfur centre
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
selenate
-
mixed-type inhibition
Thiocyanate
-
mixed-type inhibition
tungstate
-
highly inhibitory
tungstate
-
in vitro and in vivo
tungstate
-
SER isolated from periplasmic fractions from cells grown on 1 mM tungstate display selenate reductase activities with a 20fold reduction in Vmax and a 23fold increase in substrate binding affinity. The thermo-stability and pH dependence of tungsten-SER is shown to be similar to that observed for molybdenum-SER
additional information
-
no inhibition by nitrate
-
additional information
-
no inhibition by sodium azide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
selenate
-
induction of enzyme activity when included in growth medium
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.25
-
benzyl viologen
-
20C
0.0007
-
selenate
-
tungsten-SER, pH and temperature not specified in the publication, Vmax: 0.01 micromol/min/mg
0.016
-
selenate
-
pH 6.0
0.016
-
selenate
-
-
0.016
-
selenate
-
molybdenum-SER, pH and temperature not specified in the publication, Vmax: 0.2 micromol/min/mg
2
-
selenate
-
using electron donormethyl viologen
2.1
-
selenate
-
pH 7.2, 30C, holenzyme complex
5.5
-
selenate
-
pH 7.2, 30C, isolated alpha subunit
6.25
-
selenate
-
with reduced benzyl viologen, 20C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5
-
selenate
-
using electron donormethyl viologen
387
-
selenate
-
pH 6.0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
Thiocyanate
-
30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.29
-
-
membrane fraction
0.42
-
Q9S1H0 and Q9S1G9 and Q9S1G7
wild-type
0.76
-
-
wild-type, cells grown on nitrate
1.6
-
-
wild-type, cells grown on selenate + nitrate
3.84
-
-
wild-type, cells grown on selenate
41.4
-
-
purified enzyme
500
-
-
pH 7.2, 30C
additional information
-
-
activity in nirate reductase deficient mutants under different growth conditions
additional information
-
-
microtiter plate assay method based on enzyme-dependent reoxidation of reduced methyl viologen detected at 600 nm. Assay is fast and allows for simultaneous testing of a range of alternative substrates and multiple samples
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
65
-
-
optimal temperature for molybdenum-SER
80
-
-
optimal temperature for tungsten-SER is higher than 80C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
maximal growth at a pH range of pH 9.0-11.0
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
with localisation of the catalytic site to the periplasmic side of the membrane
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
-
with localisation of the catalytic site to the periplasmic side of the membrane
-
-
Manually annotated by BRENDA team
-
loosely associated with the cytoplasmic membrane
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1, Enterobacter cloacae SLDa-1
-
-
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1, Enterobacter cloacae SLDa-1, Sulfurospirillum barnesii SES-3
-
-
-
Manually annotated by BRENDA team
additional information
-
not in the cytosol
-
Manually annotated by BRENDA team
additional information
Enterobacter cloacae SLD1a-1
-
not in the cytosol
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
160000
-
-
-
180000
-
-
gel filtration
180000
-
-
-
600000
-
-
gel filtration
700000
-
-
native gel electrophoresis of cell-free extracts and activity stain
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nonamer
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
nonamer
Enterobacter cloacae SLD1a-1
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
-
tetramer
-
1 * 82000 + 1 * 53000 + 1 *34000 + 1* 21000
tetramer
-
alphabetagammadelta, 1 * 82000 + 1 * 53000 + 1 * 34000 + 1 * 21000
tetramer
-
1 * 82000 + 1 * 53000 + 1 *34000 + 1* 21000
-
trimer
-
1 * 96000, alpha, + 1 * 40000, beta, + 1 * 23000, gamma, SDS-PAGE
trimer
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
trimer
-
alphabetagamma, 1 * 96000 + 1 * 40000 + 1 * 23000
trimer
-
alpha, beta, gamma
trimer
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
additional information
-
1 cytochrome b per alphabetagamma-complex
additional information
-
the gamma subunit may be identical with the cytochrome b
additional information
-
heterotrimeric complex: apparent about 600000 Da (3 alpha-subunits + 3 beta-subunits + 3 gamma-subunits), alpha-subunit: about 100000 Da, beta-subunit: about 55000 Da, gamma-subunit: about 36000 Da
additional information
Enterobacter cloacae SLD1a-1
-
heterotrimeric complex: apparent about 600000 Da (3 alpha-subunits + 3 beta-subunits + 3 gamma-subunits), alpha-subunit: about 100000 Da, beta-subunit: about 55000 Da, gamma-subunit: about 36000 Da
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop vapour diffusion method, precipitation by ammonium sulfate, protein solution: 10 mg/ml, 0.3-0.5 M ammonium sulfate, 50 mM piperazine, pH 6.0, reservoir solution: 1.8-2.2 M ammonium sulfate, 100 mM Tris-HCl, pH 8.0-8.9, 293 K, 2-4 weeks, cryoprotection by 25% glycerol, X-ray structure determination and analysis
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
purified molybdenum-SER complex is stable and active upon heat-shock incubation for 10 min at temperatures up to 60C. At temperatures greater than 65C all three subunits (SerABC) are readily denatured
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, enzyme extracted with Thesit retains 50% activity after being frozen for prolonged periods
-
4C, enzyme extracted with Thesit remains active for 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
57fold, to near homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA sequence determination and analysis, contruction of gene bank, genomic organisationand potential function of: genes serA, serB, and serC, additional overlapping serD
Q9S1H0 and Q9S1G9 and Q9S1G7
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
construction of diverse Tn5 insertion mutants by transposon mutagenesis, overview
additional information
Q9S1H0 and Q9S1G9 and Q9S1G7
construction of Tn5 insertion mutants by transposon mutagenesis using Escherichia coli strain S17-1 as partner, loss of activity