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-MAY-2013, 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=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.
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; 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; DVIGCEI; -.
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:HAMAP.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:InterPro.
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: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: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; 6DGDH_C_like; 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 1 334 Glycerol-3-phosphate dehydrogenase
FT [NAD(P)+].
FT /FTId=PRO_1000123175.
FT NP_BIND 11 16 NAD (By similarity).
FT REGION 258 259 Substrate binding (By similarity).
FT ACT_SITE 194 194 Proton acceptor (By similarity).
FT BINDING 109 109 NAD; via amide nitrogen (By similarity).
FT BINDING 109 109 Substrate (By similarity).
FT BINDING 142 142 NAD; via amide nitrogen (By similarity).
FT BINDING 258 258 NAD (By similarity).
FT BINDING 284 284 NAD (By similarity).
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
//
