FRP_VIBHA
ID FRP_VIBHA Reviewed; 240 AA.
AC Q56691;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=NADPH-flavin oxidoreductase {ECO:0000303|PubMed:8206832};
DE EC=1.5.1.38 {ECO:0000269|PubMed:8206832};
DE AltName: Full=Flavin reductase P {ECO:0000303|PubMed:8206832};
DE AltName: Full=NADPH-FMN oxidoreductase;
GN Name=frp {ECO:0000303|PubMed:8206832};
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=MAV;
RX PubMed=8206832; DOI=10.1128/jb.176.12.3552-3558.1994;
RA Lei B., Liu M., Huang S., Tu S.-C.;
RT "Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and
RT overexpression of the gene and purification and characterization of the
RT cloned enzyme.";
RL J. Bacteriol. 176:3552-3558(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT.
RX PubMed=8885832; DOI=10.1021/bi961400v;
RA Tanner J.J., Lei B., Tu S.-C., Krause K.L.;
RT "Flavin reductase P: structure of a dimeric enzyme that reduces flavin.";
RL Biochemistry 35:13531-13539(1996).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of FMN to FMNH(2).
CC Involved in bioluminescence by providing FMNH(2) to luciferase.
CC {ECO:0000269|PubMed:8206832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.38;
CC Evidence={ECO:0000269|PubMed:8206832};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for NADPH {ECO:0000269|PubMed:8206832};
CC KM=7 uM for FMN {ECO:0000269|PubMed:8206832};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8885832}.
CC -!- SIMILARITY: Belongs to the flavin oxidoreductase frp family.
CC {ECO:0000305}.
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DR EMBL; U08996; AAA21331.1; -; Genomic_DNA.
DR PDB; 1BKJ; X-ray; 1.80 A; A/B=1-240.
DR PDB; 2BKJ; X-ray; 2.08 A; A/B=1-240.
DR PDBsum; 1BKJ; -.
DR PDBsum; 2BKJ; -.
DR AlphaFoldDB; Q56691; -.
DR SMR; Q56691; -.
DR STRING; 669.AL538_18210; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR KEGG; ag:AAA21331; -.
DR BioCyc; MetaCyc:MON-16933; -.
DR BRENDA; 1.5.1.38; 6632.
DR SABIO-RK; Q56691; -.
DR EvolutionaryTrace; Q56691; -.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR CDD; cd02146; NfsA-like; 1.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR016446; Flavin_OxRdtase_Frp.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR PANTHER; PTHR43425; PTHR43425; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR PIRSF; PIRSF005426; Frp; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; Luminescence;
KW NADP; Oxidoreductase.
FT CHAIN 1..240
FT /note="NADPH-flavin oxidoreductase"
FT /id="PRO_0000205508"
FT BINDING 11..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:8885832,
FT ECO:0007744|PDB:1BKJ"
FT BINDING 39
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:8885832,
FT ECO:0007744|PDB:1BKJ"
FT BINDING 67..69
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:8885832,
FT ECO:0007744|PDB:1BKJ"
FT BINDING 128..131
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:8885832,
FT ECO:0007744|PDB:1BKJ"
FT BINDING 167..169
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:8885832,
FT ECO:0007744|PDB:1BKJ"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1BKJ"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1BKJ"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 98..121
FT /evidence="ECO:0007829|PDB:1BKJ"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:1BKJ"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1BKJ"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:1BKJ"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:1BKJ"
SQ SEQUENCE 240 AA; 26310 MW; 7EB9913D9BB0833E CRC64;
MNNTIETILA HRSIRKFTAV PITDEQRQTI IQAGLAASSS SMLQVVSIVR VTDSEKRNEL
AQFAGNQAYV ESAAEFLVFC IDYQRHATIN PDVQADFTEL TLIGAVDSGI MAQNCLLAAE
SMGLGGVYIG GLRNSAAQVD ELLGLPENSA VLFGMCLGHP DQNPEVKPRL PAHVVVHENQ
YQELNLDDIQ SYDQTMQAYY ASRTSNQKLS TWSQEVTGKL AGESRPHILP YLNSKGLAKR
