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Database: UniProt/TrEMBL
Entry: E8XEC6_SALT4
LinkDB: E8XEC6_SALT4
Original site: E8XEC6_SALT4 
ID   E8XEC6_SALT4            Unreviewed;       542 AA.
AC   E8XEC6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN   Name=glpA {ECO:0000313|EMBL:ADX18044.1};
GN   OrderedLocusNames=STM474_2380 {ECO:0000313|EMBL:ADX18044.1};
OS   Salmonella typhimurium (strain 4/74).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX18044.1, ECO:0000313|Proteomes:UP000008978};
RN   [1] {ECO:0000313|EMBL:ADX18044.1, ECO:0000313|Proteomes:UP000008978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX   PubMed=21478351; DOI=10.1128/JB.00394-11;
RA   Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA   Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT   "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT   Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT   animals.";
RL   J. Bacteriol. 193:3162-3163(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000153,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005157}.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC. {ECO:0000256|ARBA:ARBA00011331}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
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DR   EMBL; CP002487; ADX18044.1; -; Genomic_DNA.
DR   RefSeq; WP_000857292.1; NC_016857.1.
DR   AlphaFoldDB; E8XEC6; -.
DR   KEGG; seb:STM474_2380; -.
DR   PATRIC; fig|909946.3.peg.2428; -.
DR   HOGENOM; CLU_015740_0_1_6; -.
DR   OMA; GVMTIMN; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000008978; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   InterPro; IPR017752; G3P_DH_GlpA_su.
DR   NCBIfam; TIGR03377; glycerol3P_GlpA; 1.
DR   PANTHER; PTHR11985:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217}.
FT   DOMAIN          10..359
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          432..484
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   542 AA;  59029 MW;  625B4BE306EA8C65 CRC64;
     MKTRDSQTSD VIIIGGGATG AGIARDCALR GLRVILVERH DIATGATGRN HGLLHSGARY
     AVTDAESARE CISENQILKR IARHCVEPTD GLFITLPEDD LAFQATFIRA CEAAGIRAEA
     IDPQQARIIE PSVNPALIGA VKVPDGTVDP FRLTAANMLD AREHGAIVLT AHEVTGLIRE
     GATVCGVHVR NHLTGETQTL HAPVVVNAAG IWGQQIAEYA DLSIRMFPAK GSLLIMDHRI
     NQHVINRCRK PSDADILVPG DTISLIGTTS THIDYNEIDS NRVTADEVDI LLREGEKLAP
     VMAKTRILRA YSGVRPLVAS DDDPSGRNVS RGIVLFDHAE RDGLDGFITI TGGKLMTYRL
     MAEWATDAVC RKLGNTRPCI TADTPLPGSK ESTEHTLKRI ISLPAPLRGS AVYRHGDRTP
     GWLSEGRQHR SLVCECEAVT AGEVQYAVEN LTVNSLLDLR RRTRVGMGTC QGELCACRAA
     GLLQRFNVTT AAQSITQLSE FLNERWKGVQ PVAWGDALRE SEFTRWVYQG LCGLEKEHQD
     EI
//
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