ID   NPHA1_RHOSO             Reviewed;         519 AA.
AC   Q8RQQ0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=4-nitrophenol 2-monooxygenase, oxygenase component;
DE            EC=1.14.13.29;
DE   AltName: Full=4-nitrophenol hydroxylase;
DE            Short=4-NP hydroxylase;
DE   AltName: Full=Two-component 4-nitrophenol hydroxylase;
GN   Name=nphA1;
OS   Rhodococcus sp.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE DEGRADATION OF
RP   4-NITROPHENOL.
RC   STRAIN=PN1;
RX   PubMed=16233382; DOI=10.1263/jbb.95.139;
RA   Takeo M., Yasukawa T., Abe Y., Niihara S., Maeda Y., Negoro S.;
RT   "Cloning and characterization of a 4-nitrophenol hydroxylase gene cluster
RT   from Rhodococcus sp. PN1.";
RL   J. Biosci. Bioeng. 95:139-145(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A 4-NITROPHENOL
RP   2-MONOOXYGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, INDUCTION, AND
RP   SUBUNIT.
RC   STRAIN=PN1;
RX   PubMed=18805976; DOI=10.1128/jb.00742-08;
RA   Takeo M., Murakami M., Niihara S., Yamamoto K., Nishimura M., Kato D.,
RA   Negoro S.;
RT   "Mechanism of 4-nitrophenol oxidation in Rhodococcus sp. Strain PN1:
RT   characterization of the two-component 4-nitrophenol hydroxylase and
RT   regulation of its expression.";
RL   J. Bacteriol. 190:7367-7374(2008).
CC   -!- FUNCTION: Utilizes the flavins supplied by NphA2 to catalyze the
CC       degradation of 4-nitrophenol (4-NP) via 4-nitrocatechol (4-NC) which is
CC       used as the sole carbon, nitrogen, and energy source. Can also degrade
CC       phenol and 4-chlorophenol as rapidly as 4-NP.
CC       {ECO:0000269|PubMed:16233382, ECO:0000269|PubMed:18805976}.
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:18805976};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:18805976};
CC   -!- ACTIVITY REGULATION: Partially inhibited by concentrations of FAD above
CC       10 uM and completely inhibited by concentrations above 50 uM.
CC       {ECO:0000269|PubMed:18805976}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:18805976};
CC   -!- SUBUNIT: Homotetramer. 4-nitrophenol 2-monooxygenase complex consists
CC       of an oxygenase component NphA1 and a flavin reductase component NphA2.
CC       {ECO:0000269|PubMed:18805976}.
CC   -!- INDUCTION: By 4-NP in the presence of NphR.
CC       {ECO:0000269|PubMed:18805976}.
CC   -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB081773; BAB86378.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RQQ0; -.
DR   SMR; Q8RQQ0; -.
DR   BioCyc; MetaCyc:MON-13017; -.
DR   BRENDA; 1.14.13.29; 10870.
DR   GO; GO:0018601; F:4-nitrophenol 2-monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0046196; P:4-nitrophenol catabolic process; IDA:UniProtKB.
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; IPR024677; HpaB/PvcC.
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   PIRSF; PIRSF500125; 4_HPA_large; 1.
DR   PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..519
FT                   /note="4-nitrophenol 2-monooxygenase, oxygenase component"
FT                   /id="PRO_0000418987"
SQ   SEQUENCE   519 AA;  58038 MW;  B1D7FA270D196A2C CRC64;
     MTTSAFVDDR VGVPNDVRPM TGDEYLESLR DGREVYFRGE RVDDVTTHPA FRNSARSVAR
     MYDALHQPEQ EGVLAVPTDT GNGGFTHPFF KTARSADDLV LSRDAIVAWQ REVYGWLGRS
     PDYKASFLGT LGANADFYGP YRDNALRWYK HAQERMLYLN HAIVNPPIDR DKPADETADV
     CVHVVEETDA GLIVSGAKVV ATGSAITNAN FIAHYGLLRK KEYGLIFTVP MDSPGLKLFC
     RTSYEMNAAV MGTPFDYPLS SRFDENDAIM VFDRVLVPWE NVFAYDTDTA NGFVMKSGFL
     SRFMFHGCAR LAVKLDFIAG CVMKGVEMTG SAGFRGVQMQ IGEILNWRDM FWGLSDAMAK
     SPEQWVNGAV QPNLNYGLAY RTFMGVGYPR VKEIIQQVLG SGLIYLNSHA SDWANPAMRP
     YLDQYVRGSN GVAAIDRVQL LKLLWDAVGT EFGGRHELYE RNYGGDHEAV RFQTLFAYQA
     TGQDLALKGF AEQCMSEYDV DGWTRPDLIG NDDLRIVRG