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Database: UniProt/TrEMBL
Entry: B1LI86_ECOSM
LinkDB: B1LI86_ECOSM
Original site: B1LI86_ECOSM 
ID   B1LI86_ECOSM            Unreviewed;       501 AA.
AC   B1LI86;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   25-OCT-2017, entry version 67.
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:ACB18226.1};
GN   OrderedLocusNames=EcSMS35_3706 {ECO:0000313|EMBL:ACB18226.1};
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB18226.1, ECO:0000313|Proteomes:UP000007011};
RN   [1] {ECO:0000313|EMBL:ACB18226.1, ECO:0000313|Proteomes:UP000007011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia
RT   coli SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB18226.1; -; Genomic_DNA.
DR   RefSeq; WP_000448165.1; NC_010498.1.
DR   ProteinModelPortal; B1LI86; -.
DR   EnsemblBacteria; ACB18226; ACB18226; EcSMS35_3706.
DR   KEGG; ecm:EcSMS35_3706; -.
DR   HOGENOM; HOG000004811; -.
DR   KO; K00111; -.
DR   OMA; WSSKLAH; -.
DR   Proteomes; UP000007011; 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:UP000007011};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217,
KW   ECO:0000313|EMBL:ACB18226.1}.
FT   DOMAIN        5    323       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      381    497       DAO_C. {ECO:0000259|Pfam:PF16901}.
SQ   SEQUENCE   501 AA;  56735 MW;  2B0F2126D62569E3 CRC64;
     METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE
     FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS
     TGLRFGANSV LKPEIKRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATSARRENG
     LWIVEAEDID TGKKYTWQAR GLVNATGPWV KQFFDDGMHL PSPYGIRLIK GSHIVVPRVH
     TQKQAYILQN EDKRIVFVIP WMDEFSIIGT TDVEYKGDPK AVKIEESEIN YLLKVYNTHF
     KKQLSRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK
     LAEHALEKLT PYYQGIGPAW TKESVLPGGA IEGDRDDYAA RLRRRYPFLT ESLARHYART
     YGSNSELLLG NAGAISDLGE DFGHEFYEAE LKYLVDHEWV RRADDALWRR TKQGMWLNAD
     QQSRVSQWLV EYTQQKLSLA S
//
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