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Database: UniProt
Entry: A9R691
LinkDB: A9R691
Original site: A9R691 
ID   GPDA_YERPG              Reviewed;         339 AA.
AC   A9R691;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   14-MAY-2014, entry version 57.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+];
DE            EC=1.1.1.94;
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
GN   Name=gpsA; OrderedLocusNames=YpAngola_A0073;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/JB.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y.,
RA   Mou S., Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola
RT   reveals new insights into the evolution and pangenome of the plague
RT   bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) =
CC       glycerone phosphate + NAD(P)H.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; CP000901; ABX86514.1; -; Genomic_DNA.
DR   RefSeq; YP_001604712.1; NC_010159.1.
DR   ProteinModelPortal; A9R691; -.
DR   STRING; 349746.YpAngola_A0073; -.
DR   EnsemblBacteria; ABX86514; ABX86514; YpAngola_A0073.
DR   GeneID; 5798538; -.
DR   KEGG; ypg:YpAngola_A0073; -.
DR   PATRIC; 18568969; VBIYerPes97331_0320.
DR   eggNOG; COG0240; -.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; CHRAFLP; -.
DR   OrthoDB; EOG6JDWF4; -.
DR   BioCyc; YPES349746:GHPB-75-MONOMER; -.
DR   UniPathway; UPA00940; -.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0036439; F:glycerol-3-phosphate dehydrogenase [NADP+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR11728; PTHR11728; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW   NAD; Oxidoreductase; Phospholipid biosynthesis;
KW   Phospholipid metabolism.
FT   CHAIN         1    339       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_1000123207.
FT   NP_BIND      12     17       NAD (By similarity).
FT   REGION      259    260       Substrate binding (By similarity).
FT   ACT_SITE    195    195       Proton acceptor (By similarity).
FT   BINDING     110    110       NAD; via amide nitrogen (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     143    143       NAD; via amide nitrogen (By similarity).
FT   BINDING     259    259       NAD (By similarity).
FT   BINDING     285    285       NAD (By similarity).
SQ   SEQUENCE   339 AA;  36194 MW;  BD559B0B48242F3E CRC64;
     MNTNPASMAV IGAGSYGTAL AITLARNGHQ VVLWGHDPKH IQQLQQDRCN RAFLPDAAFP
     DTLRLETDLA CALAASRDVL VVVPSHVFGA VLHQLKPHLR KDARIVWATK GLEAETGRLL
     QDVAREVLGE AIPLAVISGP TFAKELAAGL PTAIALASTD VQFSEDLQQL LHCGKSFRVY
     SNPDFIGVQL GGAVKNVIAI GAGMSDGIGF GANARTALIT RGLAEMTRLG TALGADPSTF
     MGMAGLGDLV LTCTDNQSRN RRFGIMLGQG LGVKEAQDNI GQVVEGYRNT KEVLALAQRH
     GVEMPITEQI YQVLYCHKNA REAALTLLGR TKKDEKIGI
//
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