KEGG   ENZYME: 1.7.2.9
Entry
EC 1.7.2.9                  Enzyme                                 
Name
hydroxylamine oxidase;
HOX
Class
Oxidoreductases;
Acting on other nitrogenous compounds as donors;
With a cytochrome as acceptor
Sysname
hydroxylamine:ferricytochrome-c oxidoreductase (nitric acid-forming)
Reaction(IUBMB)
hydroxylamine + 3 ferricytochrome c = nitric oxide + 3 ferrocytochrome c + 3 H+ [RN:R10165]
Reaction(KEGG)
R10165
Substrate
hydroxylamine [CPD:C00192];
ferricytochrome c [CPD:C00125]
Product
nitric oxide [CPD:C00533];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080]
Comment
The enzyme, characterized from the anaerobic ammonium-oxidizing (anammox) bacterium Kuenenia stuttgartiensis, is very similar to EC 1.7.2.6, hydroxylamine dehydrogenase. Both enzymes are homotrimeric enzymes in which each subunit contains seven c-type hemes and one specialized P460-type heme that is bound to a tyrosine residue in an adjacent subunit. However, this enzyme catalyses only the 3 electron oxidation of hydroxylamine, forming nitric oxide, and is not capable of performing further oxidation to form nitrite.
History
EC 1.7.2.9 created 2021
Orthology
K00378  hydroxylamine oxidase
Genes
EPSL0Y14_05540
GSUBKP001_11225 KP001_15375
GPLM1B72_16530
DHRLGS26_03465 LGS26_05705
KSTKSMBR1_2670(hao_3) KSMBR1_3040(hao_4)
BROCIPI25_10100 IPI25_12655
BPITBPIT_00280 BPIT_07270 BPIT_12320
JETL3J17_05730 L3J17_08095 L3J17_10510
Reference
1  [PMID:24302732]
  Authors
Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B.
  Title
Structural basis of biological NO generation by octaheme oxidoreductases.
  Journal
J Biol Chem 289:1228-42 (2014)
DOI:10.1074/jbc.M113.525147
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.7.2.9
IUBMB Enzyme Nomenclature: 1.7.2.9
ExPASy - ENZYME nomenclature database: 1.7.2.9
BRENDA, the Enzyme Database: 1.7.2.9
CAS: 9075-43-8

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