FRE_VIBHA
ID FRE_VIBHA Reviewed; 237 AA.
AC P43127;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
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 Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21; 163-178
RP AND 226-236.
RC STRAIN=ATCC 14126 / NBRC 15634 / NCIMB 1280;
RX PubMed=8167139; DOI=10.1016/0005-2728(94)90216-x;
RA Izumoto Y., Mori T., Yamamoto T.;
RT "Cloning and nucleotide sequence of the gene for NADH:FMN oxidoreductase
RT from Vibrio harveyi.";
RL Biochim. Biophys. Acta 1185:243-246(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-204.
RC STRAIN=ATCC 33843 / NCIMB 1871 / 392 / MAV;
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).
RN [3]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=6981058; DOI=10.1007/bf00238506;
RA Watanabe H., Hastings J.W.;
RT "Specificities and properties of three reduced pyridine nucleotide-flavin
RT mononucleotide reductases coupling to bacterial luciferase.";
RL Mol. Cell. Biochem. 44:181-187(1982).
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; D14674; BAA03505.1; -; Genomic_DNA.
DR EMBL; D17746; BAA04598.1; -; Genomic_DNA.
DR RefSeq; WP_009696790.1; NZ_UAVF01000002.1.
DR AlphaFoldDB; P43127; -.
DR SMR; P43127; -.
DR STRING; 669.AL538_09195; -.
DR GeneID; 57819637; -.
DR OrthoDB; 1834577at2; -.
DR BioCyc; MetaCyc:MON-16662; -.
DR BRENDA; 1.5.1.39; 6632.
DR BRENDA; 1.5.1.42; 6632.
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 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Luminescence; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6981058,
FT ECO:0000269|PubMed:8167139"
FT CHAIN 2..237
FT /note="NAD(P)H-flavin reductase"
FT /id="PRO_0000068150"
FT DOMAIN 2..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 237 AA; 26483 MW; ABC7AF98861A4C3B CRC64;
MTIQCKVKSI QPLACNTYQI LLHPESPVPF KAGQYLMVVM GEKDKRPFSI ASSPCRHEGE
LELHIGAAEH NAYALEVVEA MQAALETDGH IEIDAPHGDA WVQEESERPL LLIAGGTGFS
YVRSILDHCV AQNKTNPIYL YWGARDNCQL YAKEELVEIA DKFANVHFVP VVEEAPADWQ
GKVGNVLQAV SEDFESLENY DIYIAGRFEM AGAAREQFTQ NKKAKSERMF ADAYAFI
