NPCA_RHOOP
ID NPCA_RHOOP Reviewed; 528 AA.
AC Q6F4M8;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase, oxygenase 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=npcA;
OS Rhodococcus opacus (Nocardia opaca).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=37919;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP INDUCTION, SUBUNIT, AND 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, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:9647818};
CC -!- ACTIVITY REGULATION: Inhibited by methimazole.
CC {ECO:0000269|PubMed:9647818}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene completely lose the
CC ability to grow on 4-NP, 4-NCA, and hydroxyquinol.
CC {ECO:0000269|PubMed:15262926}.
CC -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AB154422; BAD30042.1; -; Genomic_DNA.
DR RefSeq; WP_007295637.1; NZ_CP051855.1.
DR AlphaFoldDB; Q6F4M8; -.
DR SMR; Q6F4M8; -.
DR KEGG; ag:BAD30042; -.
DR BioCyc; MetaCyc:MON-17435; -.
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:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR PANTHER; PTHR36117; PTHR36117; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase; NAD;
KW Oxidoreductase.
FT CHAIN 1..528
FT /note="4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-
FT monooxygenase, oxygenase component"
FT /id="PRO_0000422327"
FT BINDING 100..104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153..155
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 159..162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 461..464
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 59739 MW; 9E4CA3E664B57C01 CRC64;
MRTGQQYLES LRDGRQVYVG GELIDDVTTH PKTSGYAKAI AEYYDLHLDP EHQDVLTFVD
DDGVRKSMHW FLPRSKADAA RRRAYHEFWF RHFQGGIFTR PPAGMHVVMY AQIDDPEPWG
DNAVVAGGRT ISFADNIRSQ WQRVTTDDVA LSPMFVDVQF DRGRDDALVE TPMLSIVEQN
DQGIVVRGWK AMGTSLPFVN ELLVGNLWRP GQTSDQTVYA IVPVNTPGLS LVCRQSNATP
DADPYDHPLS TIGDELDGMA YFDDVFIPWE NVQHIGNPDH AKWYPQRQFD WVHIETQIRH
AVHAELIVGL ALLLTNALGT NNNPIVQSQL ADLVRFRETC KAFAIAAEET GFTTAGGLFK
PNNIYVDLGR AHYLENIHNA VNQLIEFCGR GVVMSPTKAD FDHPFLGPKL EEALRGTSIS
ARDRVSIFRQ ISERYLTQWG ARHEMFEKFN GTPLYLVRLL TMQRTEYQVD GPLTDLARQV
LGFGDTEALA ARAAEVEKNS NWASVAYQPE YAREQDVRDG YYKETEKV
