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Database: UniProt/TrEMBL
Entry: W8ZXH7_ECOLX
LinkDB: W8ZXH7_ECOLX
Original site: W8ZXH7_ECOLX 
ID   W8ZXH7_ECOLX            Unreviewed;       506 AA.
AC   W8ZXH7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   25-OCT-2017, entry version 25.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   Name=glpD {ECO:0000313|EMBL:CDN84163.1};
GN   ORFNames=EC958_3818 {ECO:0000313|EMBL:CDN84163.1};
OS   Escherichia coli O25b:H4-ST131.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=941322 {ECO:0000313|EMBL:CDN84163.1, ECO:0000313|Proteomes:UP000032727};
RN   [1] {ECO:0000313|EMBL:CDN84163.1, ECO:0000313|Proteomes:UP000032727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC958 {ECO:0000313|EMBL:CDN84163.1,
RC   ECO:0000313|Proteomes:UP000032727};
RX   PubMed=25126841; DOI=10.1371/journal.pone.0104400;
RA   Forde B.M., Ben Zakour N.L., Stanton-Cook M., Phan M.D., Totsika M.,
RA   Peters K.M., Chan K.G., Schembri M.A., Upton M., Beatson S.A.;
RT   "The complete genome sequence of Escherichia coli EC958: a high
RT   quality reference sequence for the globally disseminated multidrug
RT   resistant E. coli O25b:H4-ST131 clone.";
RL   PLoS ONE 9:e104400-e104400(2014).
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; HG941718; CDN84163.1; -; Genomic_DNA.
DR   ProteinModelPortal; W8ZXH7; -.
DR   EnsemblBacteria; CDN84163; CDN84163; EC958_3818.
DR   KEGG; ecos:EC958_3818; -.
DR   KO; K00111; -.
DR   Proteomes; UP000032727; 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   InterPro; IPR031656; DAO_C.
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:UP000032727};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217}.
FT   DOMAIN       10    328       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      386    496       DAO_C. {ECO:0000259|Pfam:PF16901}.
SQ   SEQUENCE   506 AA;  57313 MW;  EEAEBA966121684E CRC64;
     MNEGSMETKD LIVIGGGING AGIAADAAGR GLSVLMLEAQ DLACATSSAS SKLIHGGLRY
     LEHYEFRLVS EALAEREVLL KMAPHIAFPM RFRLPHRPHL RPAWMIRIGL FMYDHLGKRT
     SLPGSTGLRF GANSVLKPEI KRGFEYSDCW VDDARLVLAN AQMVVRKGGE VLTRTRATSA
     RRENGLWIVE AEDIDTGKKY TWQARGLVNA TGPWVKQFFD DGMHLPSPYG IRLIKGSHIV
     VPRVHTQKQA YILQNEDKRI VFVIPWMDEF SIIGTTDVEY KGDPKAVKIE ESEINYLLKV
     YNTHFKKQLS RDDIVWTYSG VRPLCDDESD SPQAITRDYT LDIHDENGKA PLLSVFGGKL
     TTYRKLAEHA LEKLTPYYQG IGPAWTKESV LPGGAIEGDR DDYAARLRRR YPFLTESLAR
     HYARTYGSNS ELLLGNAGAI SDLGEDFGHE FYEAELKYLV DHEWVRRADD ALWRRTKQGM
     WLNADQQSRV SQWLMEYTQQ RLSLAS
//
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