ID   LUXG_VIBHA              Reviewed;         233 AA.
AC   P16447;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable flavin reductase;
DE            EC=1.-.-.-;
GN   Name=luxG;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2303459; DOI=10.1016/s0021-9258(19)39798-4;
RA   Swartzman E., Miyamoto C., Graham A., Meighen E.;
RT   "Delineation of the transcriptional boundaries of the lux operon of Vibrio
RT   harveyi demonstrates the presence of two new lux genes.";
RL   J. Biol. Chem. 265:3513-3517(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX   PubMed=2775296; DOI=10.1016/0006-291x(89)92103-7;
RA   Johnston T.C., Hruska K.S., Adams L.F.;
RT   "The nucleotide sequence of the luxE gene of Vibrio harveyi and a
RT   comparison of the amino acid sequences of the acyl-protein synthetases from
RT   V. harveyi and V. fischeri.";
RL   Biochem. Biophys. Res. Commun. 163:93-101(1989).
CC   -!- FUNCTION: Probable flavin reductase in the luminescent systems of
CC       different marine bacteria.
CC   -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; M27139; AAA27537.1; -; Genomic_DNA.
DR   EMBL; M28815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B35081; B35081.
DR   RefSeq; WP_050933764.1; NZ_JPTS01001574.1.
DR   AlphaFoldDB; P16447; -.
DR   SMR; P16447; -.
DR   GeneID; 57823100; -.
DR   PATRIC; fig|669.65.peg.3624; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Luminescence; Oxidoreductase.
FT   CHAIN           1..233
FT                   /note="Probable flavin reductase"
FT                   /id="PRO_0000068143"
FT   DOMAIN          1..133
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         111..115
FT                   /ligand="pyridine"
FT                   /ligand_id="ChEBI:CHEBI:16227"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  26109 MW;  4F93E087D2E34EE2 CRC64;
     MLCSIEKIEP LTSFIFRVLL KPDQPFEFRA GQYINVSLSF GSLPFSIASC PSNGAFLELH
     IGGSDISKKN TLVMEELTNS WGCGNMVEVS EARGKAWLRD ESVKPLLLVA GGTGMSYTLS
     ILKNSLAQGF NQPIYVYWGA KDMENLYVHD ELVDIALENK NVSYVPVTEI STCPQYAKQG
     KVLECVMSDF RNLSEFDIYL CGPYKMVEVA RDWFCDKRGA EPEQLYADAF AYL