ID   FRE_ALIFS               Reviewed;         236 AA.
AC   P43126;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=NAD(P)H-flavin reductase;
DE            EC=1.5.1.-;
DE   AltName: Full=NAD(P)H:flavin oxidoreductase;
GN   Name=fre;
OS   Aliivibrio fischeri (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RX   PubMed=8206831; DOI=10.1128/jb.176.12.3544-3551.1994;
RA   Zenno S., Saigo K.;
RT   "Identification of the genes encoding NAD(P)H-flavin oxidoreductases that
RT   are similar in sequence to Escherichia coli Fre in four species of luminous
RT   bacteria: Photorhabdus luminescens, Vibrio fischeri, Vibrio harveyi, and
RT   Vibrio orientalis.";
RL   J. Bacteriol. 176:3544-3551(1994).
CC   -!- FUNCTION: Involved in bioluminescence. It is a good supplier of reduced
CC       flavin mononucleotide (FMNH2) to the bioluminescence reaction.
CC       Preferably uses riboflavin as an electron acceptor when NADPH is used
CC       as an electron donor.
CC   -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; D17744; BAA04596.1; -; Genomic_DNA.
DR   RefSeq; WP_017018910.1; NZ_WOAY01000009.1.
DR   AlphaFoldDB; P43126; -.
DR   SMR; P43126; -.
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; IPR008333; Cbr1-like_FAD-bd_dom.
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; PF00970; FAD_binding_6; 1.
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..236
FT                   /note="NAD(P)H-flavin reductase"
FT                   /id="PRO_0000068149"
FT   DOMAIN          1..103
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         115..119
FT                   /ligand="pyridine"
FT                   /ligand_id="ChEBI:CHEBI:16227"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   236 AA;  26069 MW;  7636B63DA79339AB CRC64;
     MPINCKVKSI EPLACNTFRI LLHPEQPVAF KAGQYLTVVM GEKDKRPFSI ASSPCRHEGE
     IELHIGAAEH NAYAGEVVES MKSALETGGD ILIDAPHGEA WIREDSDRSM LLIAGGTGFS
     YVRSILDHCI SQQIQKPIYL YWGGRDECQL YAKAELESIA QAHSHITFVP VVEKSEGWTG
     KTGNVLEAVK ADFNSLADMD IYIAGRFEMA GAAREQFTTE KQAKKEQLFG DAFAFI