(data stored in ACNUC7421 zone)

SWISSPROT: GPDA_PSEHT

ID   GPDA_PSEHT              Reviewed;         335 AA.
AC   Q3IIE0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 91.
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=PSHAa0370;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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}.
DR   EMBL; CR954246; CAI85468.1; -; Genomic_DNA.
DR   RefSeq; WP_011327081.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIE0; -.
DR   SMR; Q3IIE0; -.
DR   STRING; 326442.PSHAa0370; -.
DR   EnsemblBacteria; CAI85468; CAI85468; PSHAa0370.
DR   KEGG; pha:PSHAa0370; -.
DR   PATRIC; fig|326442.8.peg.354; -.
DR   eggNOG; ENOG4105CSF; Bacteria.
DR   eggNOG; COG0240; LUCA.
DR   HOGENOM; HOG000246854; -.
DR   KO; K00057; -.
DR   OMA; NMIGKGY; -.
DR   OrthoDB; POG091H060E; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000006843; Chromosome I.
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-EC.
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: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-KW.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
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   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   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IIE0.
DR   SWISS-2DPAGE; Q3IIE0.
KW   Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW   NAD; Oxidoreductase; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome.
FT   CHAIN         1    335       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+].
FT                                /FTId=PRO_0000255343.
FT   NP_BIND      12     17       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   REGION      259    260       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   ACT_SITE    195    195       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     110    110       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     110    110       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00394}.
FT   BINDING     143    143       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     259    259       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
FT   BINDING     285    285       NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   335 AA;  35484 MW;  BD8EA3380023EB6B CRC64;
     MSTATSAVTV LGAGSYGTAL AICLARNGHQ VTLWGRNSDD VATLAAERKN QRYLPDIPFP
     DTLTLEADLQ RAAASNEIVL VVVPSHAFGD TLKQIKPALQ QGAKVAWATK GLEPNTGRLL
     QEVAVQELGD AIPLAVLSGP TFAKEMAMGS PTAISVSSTS TEFAQQLADL LHCGRSFRVY
     NNDDFIGIQL GGAVKNVIAI GAGISDGVGF GANARTALIT RGLAELTRLG CALGAKPETF
     MGMAGLGDLI LTCTDNQSRN RRFGLALGKG ESVEAAIESI GQVVEGFRNT KEVYLLAQRS
     GVEMPITEQI YKVLYENKDM KEAAMALLGR EQRSE
//

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