ID   FRE_PHOLU               Reviewed;         233 AA.
AC   P43129;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 78.
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   Photorhabdus luminescens (Xenorhabdus luminescens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=29488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29999 / DSM 3368 / BCRC 14801 / CIP 106429 / NCIMB 12670 / Hb;
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; D17745; BAA04597.1; -; Genomic_DNA.
DR   RefSeq; WP_049585178.1; NZ_FMWJ01000008.1.
DR   AlphaFoldDB; P43129; -.
DR   SMR; P43129; -.
DR   STRING; 29488.KS18_11990; -.
DR   GeneID; 45658137; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..233
FT                   /note="NAD(P)H-flavin reductase"
FT                   /id="PRO_0000068148"
FT   DOMAIN          2..99
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;  26440 MW;  51439AEE1CB95B6F CRC64;
     MTTLSCKVTS VEAITDTVYR VRLLPDSPFL FRAGQYLMVV MDERDKRPFS MASTPSEKEF
     IELHIGASEL NLYAMAVMDR ILDQKVINID IPHGKAWFRK SSANPLLLIA GGTGFSYTRS
     ILLTALEEQP KRHISMYWGG RESQHLYDLA ELRLLTERYP NLKVIPVVEQ SDNGWCGRTG
     TVLKAVLEDF GSLANYDIYI AGRFEMAKIA RERFCSERDA SADSMYGDAF EFI