(data stored in ACNUC30630 zone)

SWISSPROT: GPDA_RHOPT

ID   GPDA_RHOPT              Reviewed;         329 AA.
AC   B3Q866;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 74.
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}; OrderedLocusNames=Rpal_0255;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00394};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {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; CP001096; ACE98815.1; -; Genomic_DNA.
DR   RefSeq; WP_012494017.1; NC_011004.1.
DR   SMR; B3Q866; -.
DR   PRIDE; B3Q866; -.
DR   EnsemblBacteria; ACE98815; ACE98815; Rpal_0255.
DR   KEGG; rpt:Rpal_0255; -.
DR   HOGENOM; HOG000246853; -.
DR   KO; K00057; -.
DR   OMA; NMIGKGY; -.
DR   OrthoDB; 1419877at2; -.
DR   BioCyc; RPAL395960:RPAL_RS01270-MONOMER; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001725; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] 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-UniRule.
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-UniRule.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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; IPR036291; NAD(P)-bd_dom_sf.
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; B3Q866.
DR   SWISS-2DPAGE; B3Q866.
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW   Phospholipid biosynthesis; Phospholipid metabolism.
FT   CHAIN           1..329
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]"
FT                   /id="PRO_1000123178"
FT   NP_BIND         11..16
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   REGION          254..255
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         107
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         107
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         139
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         254
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         278
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
SQ   SEQUENCE   329 AA;  33809 MW;  9DBE812BBDEFDE52 CRC64;
     MGSLNSIAVL GGGAWGTALA QTAARAGRKV TLWEHDAGNA EHLIAARESR FLPGVRLEPS
     IQVTRDLAEA ARADALLLVV PAQVLRQVVT SLQPLIAPRT PLVACAKGIE HGTHRFMTEI
     IAEAAPAAIP AILSGPSFAA DVARGLPTAV TIAATDAACA QALAQAMNSG SFRPYHSTDV
     RGVELGGATK NVLAIAAGIV EGRQLGASAL AAMTTRGFVE LVRFGKAYGA RIETMHGLSG
     LGDLTMCCST PQSRNFSFGM ALGRGEGIES AAHGKLAEGY YTAPVLLEMA QAKGIDMPIS
     TAVAAVLGGK LSVDAAIEGL LTRPLKAEE
//

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