NPHA2_RHOSO
ID NPHA2_RHOSO Reviewed; 176 AA.
AC Q8RQP9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=NADH-dependent flavin reductase;
DE EC=1.5.1.36;
DE AltName: Full=4-nitrophenol 2-monooxygenase, flavin reductase component;
DE AltName: Full=4-nitrophenol hydroxylase, flavin reductase component;
DE Short=4-NP hydroxylase, flavin reductase component;
DE AltName: Full=Two-component 4-nitrophenol hydroxylase;
GN Name=nphA2;
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 INDUCTION, AND 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: Catalyzes the reduction of FAD with the concomitant oxidation
CC of NADH. NAD is the physiological electron donor. Subsequently, the
CC reduced flavins diffuse to the oxygenase component NphA2.
CC {ECO:0000269|PubMed:16233382, ECO:0000269|PubMed:18805976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:31303, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:60531, ChEBI:CHEBI:62787; EC=1.5.1.36;
CC Evidence={ECO:0000269|PubMed:18805976};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58.1 uM for NADH (with 0.5 mM of FAD at 22 degrees Celsius and at
CC pH 7.5) {ECO:0000269|PubMed:18805976};
CC KM=271 uM for FAD (with 0.3 mM of NADH at 22 degrees Celsius and at
CC pH 7.5) {ECO:0000269|PubMed:18805976};
CC Vmax=17.6 umol/min/mg enzyme with NADH as substrate (with 0.5 mM of
CC FAD at 22 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:18805976};
CC Vmax=18.3 umol/min/mg enzyme with FAD as substrate (with 0.3 mM of
CC NADH at 22 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:18805976};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18805976};
CC -!- SUBUNIT: Homodimer. 4-nitrophenol 2-monooxygenase complex consists of
CC 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:0000305|PubMed:18805976}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; AB081773; BAB86379.2; -; Genomic_DNA.
DR AlphaFoldDB; Q8RQP9; -.
DR SMR; Q8RQP9; -.
DR BioCyc; MetaCyc:MON-13018; -.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0036382; F:flavin reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0052875; F:riboflavin reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0046196; P:4-nitrophenol catabolic process; IDA:UniProtKB.
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 FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..176
FT /note="NADH-dependent flavin reductase"
FT /id="PRO_0000418988"
FT BINDING 39..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 48..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 63..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 95..96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 157..160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 176 AA; 19174 MW; 932EA672E498D378 CRC64;
MTETAGELDP EVTPLHLRKA LGRFASGVTI VTTAECEDED SVHGMTANAF TSVSLDPPLV
LVSISTRAKM DTKIRETGTY GISILAGDQE PVSLHFAGAA HEPDRVRFVW RRGVPLLEGA
LVHLACTVVA SHPAGDHTLH VGRVEQLWYD DGHPLVFYTG SFRSLELLGR DEPWGF
