ID Q8EJG3_SHEON Unreviewed; 232 AA.
AC Q8EJG3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=NAD(P)H-flavin reductase Fre {ECO:0000313|EMBL:AAN53585.1};
GN Name=fre {ECO:0000313|EMBL:AAN53585.1};
GN OrderedLocusNames=SO_0504 {ECO:0000313|EMBL:AAN53585.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN53585.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN53585.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN53585.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
CC -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00038177}.
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DR EMBL; AE014299; AAN53585.1; -; Genomic_DNA.
DR RefSeq; NP_716140.1; NC_004347.2.
DR RefSeq; WP_011070849.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EJG3; -.
DR STRING; 211586.SO_0504; -.
DR PaxDb; 211586-SO_0504; -.
DR KEGG; son:SO_0504; -.
DR PATRIC; fig|211586.12.peg.487; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_7_4_6; -.
DR OrthoDB; 9806195at2; -.
DR PhylomeDB; Q8EJG3; -.
DR BioCyc; SONE211586:G1GMP-479-MONOMER; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR CDD; cd06189; flavin_oxioreductase; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR47354:SF7; NAD(P)H-FLAVIN REDUCTASE; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW Reference proteome {ECO:0000313|Proteomes:UP000008186}.
FT DOMAIN 1..98
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 232 AA; 26134 MW; B072E159CD685B2A CRC64;
MKTIRCKIEK VTPFNDAVYQ VWLTPETPLA FQAGQYLCVV MGEKDKRPFS IASAPNAEVI
ELHIGAAVSE SYPMQVVERL RNSTHIDIEA PGGDAHLRHE SIRPRLLIAG GTGFSYIKSI
VEQQIALGQQ VETTLYWGCR TQDAMYYESI ARAWHDAHPW LHFVPVVEEA TANWQGKTAN
LLAQIRQDFI SLNGYDIYIA GRFDMVGAAR EIFREMGVDE AHLYGDAFAF IK
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