Any feedback?
Information on EC 1.7.99.1 - hydroxylamine reductase
for references in articles please use BRENDA:EC1.7.99.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.7.99.1 hydroxylamine reductaseIUBMB Comments
A flavoprotein. Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. May be identical to EC 1.7.2.1, nitrite reductase (NO-forming).
Specify your search results
Word Map
- 1.7.99.1
- nitrite
- desulfovibrio
- hildenborough
- desulfuricans
-
denitrification
-
sulfate-reducing
-
ammonification
The enzyme appears in viruses and cellular organisms
Synonyms
hydroxylamine reductase, hybrid cluster protein, prismane protein, fuscoredoxin, kustc0458, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
epsilonHao
epsilonproteobacterial hydroxylamine oxidoreductase
haoA
hybrid cluster protein
reductase, hydroxylamine (acceptor)
-
-
-
-
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NH3 + H2O + acceptor = hydroxylamine + reduced acceptor
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ammonia:acceptor oxidoreductase
A flavoprotein. Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. May be identical to EC 1.7.2.1, nitrite reductase (NO-forming).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37256-42-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
hydroxylamine + reduced methyl viologen
ammonia + oxidized methyl viologen
-
-
-
-
?
hydroxylamine + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrate + reduced methylene blue
nitrite + H2O + oxidized methylene blue
-
-
-
-
r
nitrate + reduced pyocyanine
nitrite + H2O + oxidized pyocyanine
-
-
-
-
r
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
-
r
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
r
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
-
r
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
best substrate
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
best substrate
-
-
r
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
hydroxylamine reductase 1 reacts with reduced benzyl viologen, ferredoxin and FMNH2
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
FADH2, NADPH
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
reduced benzyl viologen as electron donor
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
hydroxylamine reductase 2 reacts with benzyl viologen and dithionite
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
with pyocyanine or reduced methylene blue as electron donor
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
hydroxylamine reductase 1 reacts with reduced benzyl viologen, ferredoxin and FMNH2
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
hydroxylamine reductase 2 reacts with reduced benzyl viologen
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
FADH2, NADPH
-
-
?
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
-
methyl viologen is more effective than benzyl viologen, flavin nucleotides are also utilized but to a lesser extent
-
-
?
additional information
?
-
-
the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible
-
-
?
additional information
?
-
the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible
-
-
?
additional information
?
-
-
the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible
-
-
?
additional information
?
-
-
the enzyme is not able to oxidize hydroxylamine or hydrazine
-
-
-
additional information
?
-
-
the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
?
-
-
the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible
-
-
?
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
-
r
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
r
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
-
r
hydroxylamine + ferricytochrome c
nitrite + ferrocytochrome c
-
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
-
r
hydroxylamine + ferrocytochrome c
NH3 + H2O + ferricytochrome c
-
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Iron
-
iron-chlorin protein also catalyzes methyl viologen-linked reduction of hydroxylamine and nitrite at a slower rate
Iron
-
iron containing proteins: nitrite reductase-hydroxylamine reductase 1 and hydroxylamine reductase 2
Iron
-
the enzyme contains 2.7 Fe per molecule, in the case of full occupation of a hybrid cluster and a [4Fe-4S] cluster 8 Fe/molecule can be expected
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CO
-
with reduced benzyl viologen as electron donor, reductase 1: irreversible inhibition by light, reductase 2 : reversible inhibition by light
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
hydroxylamine
-
oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C
1.4
hydroxylamine
-
oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C
1.5
hydroxylamine
oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C
1.9
hydroxylamine
-
reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C
5.3
hydroxylamine
oxidation reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C
6
hydroxylamine
-
reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C
6.6
hydroxylamine
reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C
6.75
hydroxylamine
reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C
7.4
hydroxylamine
-
reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C
16.9
hydroxylamine
-
reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C
1.5
nitrite
-
recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.03
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C
0.04
below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C
0.07
-
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C
0.1
-
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C
1
-
purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C
149
-
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C
158
-
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C
2.9
-
purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C
225
-
purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C
29
-
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C
68
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C
77
purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C
98
-
purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C
additional information
0.01
-
below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C
0.01
-
below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C
0.01
-
below, purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C
additional information
-
specific activities after different purification methods
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
additional information
-
no clear or consistent pH optima observed with hydroxylamine reductase 1 and hydroxylamine reductase 2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
iron-chlorin protein also catalyzes methyl viologen-linked reduction of hydroxylamine and that of nitrite at a slower rate
-
-
brenda
wheat, nitrite reductase and hydroxylamine reductase are distinct enzymes
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
evolution
-
the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Caminibacter mediatlanticus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview
evolution
the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Campylobacter curvus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview
evolution
-
the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Campylobacter fetus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview
evolution
-
the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Nautilia profundicola with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview
Show AA Sequence and Transmembrane Helices (9540 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W434Y
additional information
W434Y
-
site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation activity, but decreased hydroxylamine reduction and increased nitrite reduction compared to the wild-type enzyme
W434Y
site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation, but slightly reduced hydroxylamine reduction and significantly reduced nitrite reduction compared to the wild-type enzyme
W434Y
-
site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation activity, but highly increased hydroxylamine reduction and highly reduced nitrite reduction compared to the wild-type enzyme
additional information
-
introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm
additional information
introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm
additional information
-
introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm