ID GPDA_PSESM Reviewed; 341 AA.
AC Q883Y4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 84.
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=PSPTO_2213;
OS Pseudomonas syringae pv. tomato (strain DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F.,
RA Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H.,
RA Nelson W.C., Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q.,
RA Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J.,
RA Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M.,
RA Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K.,
RA Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X.,
RA Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO55729.1; -; Genomic_DNA.
DR RefSeq; NP_792034.1; NC_004578.1.
DR ProteinModelPortal; Q883Y4; -.
DR STRING; 223283.PSPTO_2213; -.
DR EnsemblBacteria; AAO55729; AAO55729; PSPTO_2213.
DR GeneID; 1183864; -.
DR KEGG; pst:PSPTO_2213; -.
DR PATRIC; 19995714; VBIPseSyr93040_2245.
DR eggNOG; COG0240; -.
DR HOGENOM; HOG000246853; -.
DR KO; K00057; -.
DR OMA; DVIGCEI; -.
DR ProtClustDB; PRK00094; -.
DR BioCyc; PSYR223283:GJIX-2258-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 1 341 Glycerol-3-phosphate dehydrogenase
FT [NAD(P)+].
FT /FTId=PRO_0000138011.
FT NP_BIND 11 16 NAD (By similarity).
FT REGION 255 256 Substrate binding (By similarity).
FT ACT_SITE 191 191 Proton acceptor (By similarity).
FT BINDING 108 108 NAD; via amide nitrogen (By similarity).
FT BINDING 108 108 Substrate (By similarity).
FT BINDING 140 140 NAD; via amide nitrogen (By similarity).
FT BINDING 255 255 NAD (By similarity).
FT BINDING 281 281 NAD (By similarity).
SQ SEQUENCE 341 AA; 36680 MW; DEDE1DE7BBE7F1A0 CRC64;
MTTQQPVAVL GGGSFGTAIA NLLAENGHQV RQWMRDPEQA EAIRVNRENP RYLKGIKVRP
EVEPVTDLTA ALEVSELIFV ALPSSALRSV LSPHIERLSG KMLVSLTKGI EAQSFKLMSQ
ILEEIVPQAR IGVLSGPNLA REIAEHALTA TVVASEDEDL CQQVQAALHG RTFRVYASND
RFGVELGGAL KNVYAIIAGM AVALDMGENT KSMLITRALA EMTRFAVSQG ANPMTFLGLA
GVGDLIVTCS SPKSRNYQVG FALGQGLSLE EAVTRLGEVA EGVNTLKVLK VKAQEVQVYM
PLVAGLHAIL FEGRTLSQVI EALMRAEPKT DVDFISITGF N
//
