NPCB_RHOOP
ID NPCB_RHOOP Reviewed; 185 AA.
AC Q6F4M9;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase, reductase component;
DE Short=4-NP/4-NCA monooxygenase;
DE EC=1.14.13.166;
DE EC=1.14.13.29;
DE AltName: Full=PNP monooxygenase;
GN Name=npcB;
OS Rhodococcus opacus (Nocardia opaca).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=37919;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, SUBUNIT, AND
RP NOMENCLATURE.
RC STRAIN=SAO101;
RX PubMed=15262926; DOI=10.1128/jb.186.15.4894-4902.2004;
RA Kitagawa W., Kimura N., Kamagata Y.;
RT "A novel p-nitrophenol degradation gene cluster from a gram-positive
RT bacterium, Rhodococcus opacus SAO101.";
RL J. Bacteriol. 186:4894-4902(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RC STRAIN=JS905;
RX PubMed=9647818; DOI=10.1128/aem.64.7.2479-2484.1998;
RA Kadiyala V., Spain J.C.;
RT "A two-component monooxygenase catalyzes both the hydroxylation of p-
RT nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in
RT Bacillus sphaericus JS905.";
RL Appl. Environ. Microbiol. 64:2479-2484(1998).
CC -!- FUNCTION: Involved in the degradation of para-nitrophenol (4-NP).
CC Catalyzes both the initial hydroxylation of 4-NP to produce 4-
CC nitrocatechol (4-NCA) and the subsequent oxidative release of the nitro
CC group from 4-NCA to produce 2-hydroxy-1,4-benzoquinone. It can also use
CC 4-nitroresorcinol as substrate with a rate of nitrite release similar
CC to that observed with the two physiological substrates, 4-PN and 4-NCA.
CC {ECO:0000269|PubMed:15262926, ECO:0000269|PubMed:9647818}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-nitrophenol + H(+) + NADH + O2 = 4-nitrocatechol + H2O +
CC NAD(+); Xref=Rhea:RHEA:12568, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57730,
CC ChEBI:CHEBI:57917, ChEBI:CHEBI:57945; EC=1.14.13.29;
CC Evidence={ECO:0000269|PubMed:9647818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-nitrocatechol + NADPH + O2 = 2-hydroxy-1,4-benzoquinone +
CC H2O + NADP(+) + nitrite; Xref=Rhea:RHEA:34307, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16301, ChEBI:CHEBI:57730,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58474;
CC EC=1.14.13.166; Evidence={ECO:0000269|PubMed:9647818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-nitrocatechol + NADH + O2 = 2-hydroxy-1,4-benzoquinone + H2O
CC + NAD(+) + nitrite; Xref=Rhea:RHEA:34311, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16301, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57730, ChEBI:CHEBI:57945, ChEBI:CHEBI:58474;
CC EC=1.14.13.166; Evidence={ECO:0000269|PubMed:9647818};
CC -!- ACTIVITY REGULATION: Inhibited by methimazole.
CC {ECO:0000269|PubMed:9647818}.
CC -!- PATHWAY: Aromatic compound metabolism.
CC -!- PATHWAY: Xenobiotic degradation.
CC -!- SUBUNIT: The 4-NP/4-NCA monooxygenase is composed of an oxygenase
CC component NpcA and a reductase component NpcB.
CC {ECO:0000305|PubMed:15262926}.
CC -!- INDUCTION: By 4-NP. {ECO:0000269|PubMed:15262926}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; AB154422; BAD30041.1; -; Genomic_DNA.
DR RefSeq; WP_063709723.1; NZ_CP051855.1.
DR AlphaFoldDB; Q6F4M9; -.
DR SMR; Q6F4M9; -.
DR KEGG; ag:BAD30041; -.
DR BioCyc; MetaCyc:MON-17434; -.
DR BRENDA; 1.14.13.166; 698.
DR GO; GO:0018592; F:4-nitrocatechol 4-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0018601; F:4-nitrophenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Monooxygenase; NAD; Oxidoreductase.
FT CHAIN 1..185
FT /note="4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-
FT monooxygenase, reductase component"
FT /id="PRO_0000422328"
SQ SEQUENCE 185 AA; 20111 MW; AFBC08A862001EAF CRC64;
MLEDPMKQNV LQPLDKAEFR NVVGHFASGV TIVTAAHDGV PYGATISAVT SLCDTPPMVL
VCLNQKLGTH AAIRKARHFT INILGEDQAS LAHTFATPGA DKFADVAVHH RQHGPRLAEA
LAYLTCRVVD DLEGGTHRIF VAEVVEAQAG TGNPLSYYRG RFGHFVPYRN AMWRTTQADN
AVSPH
