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Database: UniProt
Entry: G5SJ66_SALET
LinkDB: G5SJ66_SALET
Original site: G5SJ66_SALET 
ID   G5SJ66_SALET            Unreviewed;       226 AA.
AC   G5SJ66;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=NAD(P)H-flavin reductase {ECO:0000256|ARBA:ARBA00039732};
DE   AltName: Full=NAD(P)H:flavin oxidoreductase {ECO:0000256|ARBA:ARBA00041312};
GN   ORFNames=LTSEWAN_5777 {ECO:0000313|EMBL:EHC98147.1};
OS   Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913086 {ECO:0000313|EMBL:EHC98147.1, ECO:0000313|Proteomes:UP000003536};
RN   [1] {ECO:0000313|EMBL:EHC98147.1, ECO:0000313|Proteomes:UP000003536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-580 {ECO:0000313|EMBL:EHC98147.1,
RC   ECO:0000313|Proteomes:UP000003536};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
CC   -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00038177}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHC98147.1}.
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DR   EMBL; AFCX01001878; EHC98147.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5SJ66; -.
DR   PATRIC; fig|913086.3.peg.4474; -.
DR   Proteomes; UP000003536; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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   PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR   PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
DR   Pfam; PF00970; FAD_binding_6; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          1..112
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   226 AA;  25618 MW;  B6D64BCBF49FB55F CRC64;
     MTSVEAITDT VYRVRLVPDA AFSFRAGQYL MVVMDERDKR PFSMASTPDE KGFIELHIGA
     SELNLYAMAV MDRILKDREI VVDIPHGDAW LRDDEERPLI LIAGGTGFSY VRSILLTALA
     RNPARDVTIY WGGREEKHLY DLSELEALSV NHPNLRIEPV VEQPEEGWRG RTGTVLTAVL
     QDYGTLAGHD IYIAGRFEMA KIARDLFCHE RNAREDRLFG DAFAFI
//
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