GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0N1QTZ5_SALSV
LinkDB: A0A0N1QTZ5_SALSV
Original site: A0A0N1QTZ5_SALSV 
ID   A0A0N1QTZ5_SALSV        Unreviewed;       502 AA.
AC   A0A0N1QTZ5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   28-MAR-2018, entry version 15.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=SeSA_A3718 {ECO:0000313|EMBL:ACF89562.1};
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843 {ECO:0000313|EMBL:ACF89562.1, ECO:0000313|Proteomes:UP000001865};
RN   [1] {ECO:0000313|EMBL:ACF89562.1, ECO:0000313|Proteomes:UP000001865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633 {ECO:0000313|EMBL:ACF89562.1,
RC   ECO:0000313|Proteomes:UP000001865};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol. {ECO:0000256|RuleBase:RU361217}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU361217};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU361217}.
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DR   EMBL; CP001127; ACF89562.1; -; Genomic_DNA.
DR   RefSeq; WP_000448178.1; NC_011094.1.
DR   ProteinModelPortal; A0A0N1QTZ5; -.
DR   EnsemblBacteria; ACF89562; ACF89562; SeSA_A3718.
DR   KEGG; sew:SeSA_A3718; -.
DR   KO; K00111; -.
DR   OMA; VPYYWVG; -.
DR   BioCyc; SENT439843:GHHR-3589-MONOMER; -.
DR   Proteomes; UP000001865; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001865};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217,
KW   ECO:0000313|EMBL:ACF89562.1}.
FT   DOMAIN        5    323       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      381    476       DAO_C. {ECO:0000259|Pfam:PF16901}.
SQ   SEQUENCE   502 AA;  56907 MW;  31B93B1F5A333078 CRC64;
     METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE
     FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS
     TGVRFGADSV LKPEIVRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATAARRENG
     LWIVEAEDID TGKKYVWQAR GLVNATGPWV KQFFDEGMHL PSPYGIRLIK GSHIVVPRVH
     NQKQAYILQN EDKRIVFVIP WMEEFSIIGT TDVEYKGDPK AVKIEESEIN YLLKVYNAHF
     QKQLGRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK
     LAEHAMEKLA SYYPGIGPAW TKTCVLPGGD IDGSREDYAA KLRRRYPFLT ESLARHYSRT
     YGSNTEWILG EATSLLDLGE DFGHEFYEAE LKYLVDHEWV RRTEDAIWRR TKEGMWLTAE
     QQSRITQWLA AYVEKHQLSL AS
//
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