KEGG   ENZYME: 1.14.13.166
Entry
EC 1.14.13.166              Enzyme                                 
Name
4-nitrocatechol 4-monooxygenase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)
Reaction(IUBMB)
4-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
Substrate
4-nitrocatechol [CPD:C02235];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
2-hydroxy-1,4-benzoquinone [CPD:C07103];
nitrite [CPD:C00088];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase [1]. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase [3].
History
EC 1.14.13.166 created 2012
Orthology
K21725  4-nitrocatechol/4-nitrophenol 4-monooxygenase
K21726  4-nitrophenol 2-monooxygenase / 4-nitrocatechol 4-monooxygenase, oxygenase component
Genes
PCQ: PcP3B5_26560(pnpA)
PPUD: DW66_3565 DW66_3572
PMED: E3Z27_11075
PPSH: G5J76_09115
SACH: K0H61_17530
BYI: BYI23_E003870 BYI23_E003890
RHR: CKA34_21595
BBRA: QA636_08105
MHAR: L1P08_16280
PSIN: CAK95_18535
SPHO: C3E99_15575
SNAP: PQ455_03725
SPHB: EP837_03851
TMK: QGN29_03995
SDX: C4B68_24960
ARY: ATC04_18335
ACH: Achl_4573
AMAZ: LUW76_12450
MPRN: Q3V37_21985
BALA: DSM104299_02060(npcA)
SBAE: DSM104329_03552(npcA_2)
 » show all
Reference
1  [PMID:9647818]
  Authors
Kadiyala V, Spain JC
  Title
A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus  JS905.
  Journal
Appl Environ Microbiol 64:2479-84 (1998)
DOI:10.1128/AEM.64.7.2479-2484.1998
Reference
2  [PMID:15262926]
  Authors
Kitagawa W, Kimura N, Kamagata Y
  Title
A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101.
  Journal
J Bacteriol 186:4894-902 (2004)
DOI:10.1128/JB.186.15.4894-4902.2004
  Sequence
[ag:BAD30042 BAD30041]
Reference
3  [PMID:19218392]
  Authors
Zhang JJ, Liu H, Xiao Y, Zhang XE, Zhou NY
  Title
Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3.
  Journal
J Bacteriol 191:2703-10 (2009)
DOI:10.1128/JB.01566-08
  Sequence
[ag:ABU50908]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.166
IUBMB Enzyme Nomenclature: 1.14.13.166
ExPASy - ENZYME nomenclature database: 1.14.13.166
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.166
BRENDA, the Enzyme Database: 1.14.13.166

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Gene (26)   
   KEGG ORTHOLOGY (2)   
   KEGG GENES (24)   
Protein sequence (67)   
   UniProt (65)   
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DNA sequence (64)   
   RefSeq(nuc) (2)   
   GenBank (35)   
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Protein domain (8)   
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Enzyme (1)   
   UMBBD-EC (1)   
All databases (166)   

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