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Database: UniProt
Entry: A1SZH9
LinkDB: A1SZH9
Original site: A1SZH9 
ID   GPDA_PSYIN              Reviewed;         334 AA.
AC   A1SZH9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   01-OCT-2014, entry version 63.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394};
DE            EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394};
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394};
GN   Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394};
GN   OrderedLocusNames=Ping_3207;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Staley J., Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) =
CC       glycerone phosphate + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_00394}.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism. {ECO:0000255|HAMAP-Rule:MF_00394}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}.
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DR   EMBL; CP000510; ABM04894.1; -; Genomic_DNA.
DR   RefSeq; YP_944493.1; NC_008709.1.
DR   ProteinModelPortal; A1SZH9; -.
DR   STRING; 357804.Ping_3207; -.
DR   EnsemblBacteria; ABM04894; ABM04894; Ping_3207.
DR   GeneID; 4624816; -.
DR   KEGG; pin:Ping_3207; -.
DR   PATRIC; 23071935; VBIPsyIng103130_3546.
DR   eggNOG; COG0240; -.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; VCHEGAD; -.
DR   OrthoDB; EOG6JDWF4; -.
DR   BioCyc; PING357804:GJBJ-3316-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; Reference proteome.
FT   CHAIN         1    334       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_1000123175.
FT   NP_BIND      11     16       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   REGION      258    259       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   ACT_SITE    194    194       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     109    109       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     109    109       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     142    142       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     258    258       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     284    284       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   334 AA;  36029 MW;  B99C93EB459B59EC CRC64;
     MADNIAITVL GAGSYGSALA VSLARNGHPT LLWGHQEDHI KRLQADRENK KFLPNIKFPE
     LLTPEVNLKV CLAATRNILL VVPSHVFALV LQQIKPFLTP QHRIAWATKG LEAKTGRLLQ
     EVATDILGQH YPLAVISGPT FAMEVAKGLP TAVAVAGSES KFTQDIAALF HNNRNFRTYI
     SDDFTAVQLG GAVKNVIAIG AGLADGLGFG ANARTALITR GLAELTRLGV ALGAKESSFM
     GMAGLGDLVL TCTDNQSRNR RFGLALGQGK GINAAQIEIG QVVEGYRNTE EVYNLSHRIG
     IEMPICEQIY YVLYQDKAVK QAAMDLLSRS PKDE
//
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