DB code: D00050
| CATH domain | 1.10.780.10 : Hydroxylamine Oxidoreductase; Chain A, domain 1 | Catalytic domain |
|---|---|---|
| 1.20.850.10 : Hydroxylamine Oxidoreductase; Chain A, domain 2 | Catalytic domain | |
| E.C. | 1.7.3.4 | |
| CSA | 1fgj | |
| M-CSA | 1fgj | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq |
|---|---|---|---|
| Q50925 |
Hydroxylamine oxidoreductase
|
HAO
EC 1.7.3.4 |
NP_841035.1
(Protein)
NC_004757.1 (DNA/RNA sequence) NP_842054.1 (Protein) NC_004757.1 (DNA/RNA sequence) NP_842336.1 (Protein) NC_004757.1 (DNA/RNA sequence) |
| KEGG enzyme name |
|---|
|
hydroxylamine oxidase
HAO (ambiguous cf. EC 1.7.99.8, hydroxylamine oxidoreductase) hydroxylamine oxidoreductase (ambiguous cf. EC 1.7.99.8, hydroxylamine oxidoreductase) |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| Q50925 | HAO_NITEU | Hydroxylamine + O(2) = nitrite + H(2)O. | Homotrimer. | Periplasm. | Binds 8 heme groups per subunit. One heme group a p-460 type, the remaining 7 are c-type. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00910 | Nitrogen metabolism |
| Compound table | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||
| KEGG-id | C00032 | C00192 | C00007 | C00088 | C00001 | ||||||
| E.C. | |||||||||||
| Compound | Heme | Hydroxylamine | O2 | Nitrite | H2O | ||||||
| Type | aromatic ring (with nitrogen atoms),carboxyl group,heavy metal | amine group | others | others | H2O | ||||||
| ChEBI |
17627 26355 17627 26355 |
15429 15429 |
15379 26689 27140 15379 26689 27140 |
25567 25567 |
15377 15377 |
||||||
| PubChem |
787 787 |
977 977 |
24529 24529 |
22247451 962 22247451 962 |
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| 1fgjA01 |
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Bound:4xHEM,HEC | Unbound | Unbound | Unbound | Unbound | |
| 1fgjB01 |
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Bound:3xHEM | Unbound | Unbound | Unbound | Unbound | |
| 1fgjA02 |
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Bound:4xHEM,HEC | Unbound | Unbound | Unbound | Unbound | |
| 1fgjB02 |
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Bound:3xHEM | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1fgjA01 |
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HIS 83;HIS 160(Fe1);HIS 149;HIS 246(Fe2);HIS 99;HIS 176(Fe3);HIS 233(Fe4);HIS 243(Fe5);HIS 204(Fe6) | ||||
| 1fgjB01 |
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HIS 83;HIS 160(Fe1);HIS 149;HIS 246(Fe2);HIS 99;HIS 176(Fe3);HIS 233(Fe4);HIS 243(Fe5);HIS 204(Fe6) | ||||
| 1fgjA02 |
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HIS 323(Fe5);HIS 263(Fe6);HIS 314;HIS 459(Fe7);HIS 279;HIS 364(Fe8) | ||||
| 1fgjB02 |
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HIS 323(Fe5);HIS 263(Fe6);HIS 314;HIS 459(Fe7);HIS 279;HIS 364(Fe8) | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
p.282-283, Fig.6 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1783597 |
| Journal | J Biochem (Tokyo) |
| Year | 1991 |
| Volume | 110 |
| Pages | 681-2 |
| Authors | Mikami T, Tanaka N, Sato T, Moriyama H, Numata M, Fujiwara T, Fukumori Y, Yamanaka T, Sato M, Kakiuchi K, et al |
| Title | Crystallization and preliminary X-ray studies of hydroxylamine oxidoreductase from Nitrosomonas europaea. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) |
| Medline ID | 97249290 |
| PubMed ID | 9095195 |
| Journal | Nat Struct Biol |
| Year | 1997 |
| Volume | 4 |
| Pages | 276-84 |
| Authors | Igarashi N, Moriyama H, Fujiwara T, Fukumori Y, Tanaka N |
| Title |
The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, |
| Related PDB | 1fgj |
| Related UniProtKB | Q50925 |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9425072 |
| Journal | Biochemistry |
| Year | 1998 |
| Volume | 37 |
| Pages | 523-9 |
| Authors | Arciero DM, Golombek A, Hendrich MP, Hooper AB |
| Title | Correlation of optical and EPR signals with the P460 heme of hydroxylamine oxidoreductase from Nitrosomonas europaea. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11457010 |
| Journal | J Am Chem Soc |
| Year | 2001 |
| Volume | 123 |
| Pages | 2997-3005 |
| Authors | Hendrich MP, Petasis D, Arciero DM, Hooper AB |
| Title | Correlations of structure and electronic properties from EPR spectroscopy of hydroxylamine oxidoreductase. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
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According to the literature [2], (A) Oxygenation of NH2OH by O2, (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: |
| Created | Updated |
|---|---|
| 2004-03-24 | 2009-02-26 |