EzCatDB: D00050
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DB codeD00050
CATH domainDomain 11.10.780.10 : Hydroxylamine Oxidoreductase; Chain A, domain 1Catalytic domain
Domain 21.20.850.10 : Hydroxylamine Oxidoreductase; Chain A, domain 2Catalytic domain
E.C.1.7.3.4
CSA1fgj


Enzyme Name
UniProtKBKEGG

Q50925
Protein nameHydroxylamine oxidoreductasehydroxylamine oxidase
HAO (ambiguous
cf. EC 1.7.99.8, hydroxylamine oxidoreductase)
hydroxylamine oxidoreductase (ambiguous
cf. EC 1.7.99.8, hydroxylamine oxidoreductase)
SynonymsHAO
EC 1.7.3.4
RefSeqNP_841035.1 (Protein)
NC_004757.1 (DNA/RNA sequence)
NP_842054.1 (Protein)
NP_842336.1 (Protein)

KEGG pathways
MAP codePathways
MAP00910Nitrogen metabolism

UniProtKB:Accession NumberQ50925
Entry nameHAO_NITEU
ActivityHydroxylamine + O(2) = nitrite + H(2)O.
SubunitHomotrimer.
Subcellular locationPeriplasm.
CofactorBinds 8 heme groups per subunit. One heme group a p-460 type, the remaining 7 are c-type.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00032C00192C00007C00088C00001
CompoundHemeHydroxylamineO2NitriteH2O
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metalamine groupothersothersH2O
ChEBI17627
26355
15429
27140
26689
15379
25567
15377
PubChem
787
977
24529
962
22247451
             
1fgjA01Bound:4xHEM,HECUnboundUnboundUnboundUnbound
1fgjB01Bound:3xHEMUnboundUnboundUnboundUnbound
1fgjA02Bound:4xHEM,HECUnboundUnboundUnboundUnbound
1fgjB02Bound:3xHEMUnboundUnboundUnboundUnbound

Active-site residues
pdbCofactor-binding residues
         
1fgjA01HIS 83;HIS 160(Fe1);HIS 149;HIS 246(Fe2);HIS 99;HIS 176(Fe3);HIS 233(Fe4);HIS 243(Fe5);HIS 204(Fe6)
1fgjB01HIS 83;HIS 160(Fe1);HIS 149;HIS 246(Fe2);HIS 99;HIS 176(Fe3);HIS 233(Fe4);HIS 243(Fe5);HIS 204(Fe6)
1fgjA02HIS 323(Fe5);HIS 263(Fe6);HIS 314;HIS 459(Fe7);HIS 279;HIS 364(Fe8)
1fgjB02HIS 323(Fe5);HIS 263(Fe6);HIS 314;HIS 459(Fe7);HIS 279;HIS 364(Fe8)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.282-283, Fig.6

references
[1]
PubMed ID1783597
JournalJ Biochem (Tokyo)
Year1991
Volume110
Pages681-2
AuthorsMikami T, Tanaka N, Sato T, Moriyama H, Numata M, Fujiwara T, Fukumori Y, Yamanaka T, Sato M, Kakiuchi K, et al
TitleCrystallization and preliminary X-ray studies of hydroxylamine oxidoreductase from Nitrosomonas europaea.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID97249290
PubMed ID9095195
JournalNat Struct Biol
Year1997
Volume4
Pages276-84
AuthorsIgarashi N, Moriyama H, Fujiwara T, Fukumori Y, Tanaka N
TitleThe 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea.
Related PDB1fgj
Related UniProtKBQ50925
[3]
PubMed ID9425072
JournalBiochemistry
Year1998
Volume37
Pages523-9
AuthorsArciero DM, Golombek A, Hendrich MP, Hooper AB
TitleCorrelation of optical and EPR signals with the P460 heme of hydroxylamine oxidoreductase from Nitrosomonas europaea.
[4]
PubMed ID11457010
JournalJ Am Chem Soc
Year2001
Volume123
Pages2997-3005
AuthorsHendrich MP, Petasis D, Arciero DM, Hooper AB
TitleCorrelations of structure and electronic properties from EPR spectroscopy of hydroxylamine oxidoreductase.

comments
According to the literature [2], this enzyme catalyzes the following reactions:
(A) Oxygenation of NH2OH by O2, producing HNO2 and H2O, at heme-P460 (HEC in 1fgi):
(B) Electron transfer from heme-P460 to heme-6:
(C) Electron transfer from heme-P460 to heme-7:
(D) Electron transfer from heme-6 to heme-5:
(E) Electron transfer from heme-5 to heme-3:
(F) Electron transfer from heme-3 to heme-2:
(G) Electron transfer from heme-2 to heme-1:
(H) Electron transfer from heme-7 to heme-8:
(I) Electron transfer from heme-8 to heme-2 (of adjacent subunit):
(J) Electron transfer from heme-1 to cytochrome-c554:

createdupdated
2004-03-242009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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