KEGG ENZYME: 1.14.13.166

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

MPAF:

R5R33_01750

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

SLAA:

EUU25_00625 EUU25_00675

TMK:	QGN29_03995

SDX:	C4B68_24960

ARY:	ATC04_18335

ACH:

Achl_4573

AMAZ:

LUW76_12450

ACTQ:

OG417_51835

ARHD:

VSH64_05440

UME:	RM788_45540

ASIC:

Q0Z83_043270

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

All links

Gene (42)   
   KEGG ORTHOLOGY (2)   
   KEGG GENES (29)   
   KEGG MGENES (11)   
Protein sequence (74)   
   UniProt (62)   
   SWISS-PROT (2)   
   RefSeq(pep) (10)   
DNA sequence (80)   
   RefSeq(nuc) (9)   
   GenBank (36)   
   EMBL (35)   
Protein domain (9)   
   InterPro (9)   
Enzyme (1)   
   UMBBD-EC (1)   
All databases (206)   

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