FRA1_ALIFS
ID FRA1_ALIFS Reviewed; 218 AA.
AC P46072;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Major NAD(P)H-flavin oxidoreductase;
DE EC=1.6.99.-;
DE AltName: Full=FRASE I;
OS Aliivibrio fischeri (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RX PubMed=8206830; DOI=10.1128/jb.176.12.3536-3543.1994;
RA Zenno S., Saigo K., Kanoh H., Inouye S.;
RT "Identification of the gene encoding the major NAD(P)H-flavin
RT oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744.";
RL J. Bacteriol. 176:3536-3543(1994).
RN [2]
RP SEQUENCE REVISION TO 61 AND 213.
RA Zenno S., Saigo K., Kanoh H., Inouye S.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RX PubMed=8033996; DOI=10.1016/0014-5793(94)00528-1;
RA Inouye S.;
RT "NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio
RT fischeri ATCC 7744, is a flavoprotein.";
RL FEBS Lett. 347:163-168(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH FMN AND SUBSTRATE
RP ANALOGS, AND SUBUNIT.
RC STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RX PubMed=9654450; DOI=10.1006/jmbi.1998.1871;
RA Koike H., Sasaki H., Kobori T., Zenno S., Saigo K., Murphy M.E.,
RA Adman E.T., Tanokura M.;
RT "1.8-A crystal structure of the major NAD(P)H:FMN oxidoreductase of a
RT bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and
RT substrate-analog binding, and comparison with related flavoproteins.";
RL J. Mol. Biol. 280:259-273(1998).
CC -!- FUNCTION: Involved in bioluminescence. It is a good supplier of reduced
CC flavin mononucleotide (FMNH2) to the bioluminescence reaction. Major
CC FMN reductase. It is capable of using both NADH and NADPH as electron
CC donors. As electron acceptor, FMN is the most effective, FAD is
CC considerably effective, and riboflavin is the least effective.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9654450}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; D17743; BAA04595.2; -; Genomic_DNA.
DR PIR; S46241; S46241.
DR PDB; 1V5Y; X-ray; 1.90 A; A/B=2-218.
DR PDB; 1V5Z; X-ray; 2.00 A; A/B=2-218.
DR PDB; 1VFR; X-ray; 1.80 A; A/B=1-218.
DR PDBsum; 1V5Y; -.
DR PDBsum; 1V5Z; -.
DR PDBsum; 1VFR; -.
DR AlphaFoldDB; P46072; -.
DR SMR; P46072; -.
DR DrugBank; DB03410; 4-hydroxycoumarin.
DR DrugBank; DB03247; Flavin mononucleotide.
DR DrugBank; DB01650; trans-2-hydroxycinnamic acid.
DR EvolutionaryTrace; P46072; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR CDD; cd02149; NfsB-like; 1.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR033878; NfsB-like.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; FMN;
KW Luminescence; NAD; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..218
FT /note="Major NAD(P)H-flavin oxidoreductase"
FT /id="PRO_0000072714"
FT BINDING 12..16
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 73
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 154..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 165..166
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 206..208
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1V5Y"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:1VFR"
FT TURN 176..182
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:1VFR"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1VFR"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1VFR"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1VFR"
SQ SEQUENCE 218 AA; 24721 MW; AC223CF8CEE5A636 CRC64;
MTHPIIHDLE NRYTSKKYDP SKKVSQEDLA VLLEALRLSA SSINSQPWKF IVIESDAAKQ
RMHDSFANMH QFNQPHIKAC SHVILFANKL SYTRDDYDVV LSKAVADKRI TEEQKEAAFA
SFKFVELNCD ENGEHKAWTK PQAYLALGNA LHTLARLNID STTMEGIDPE LLSEIFADEL
KGYECHVALA IGYHHPSEDY NASLPKSRKA FEDVITIL
