ID   GPDA_HELPY              Reviewed;         312 AA.
AC   O25614;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 146.
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=HP_0961;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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}.
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DR   EMBL; AE000511; AAD08003.1; -; Genomic_DNA.
DR   PIR; A64640; A64640.
DR   RefSeq; NP_207753.1; NC_000915.1.
DR   RefSeq; WP_000401714.1; NC_018939.1.
DR   AlphaFoldDB; O25614; -.
DR   SMR; O25614; -.
DR   DIP; DIP-3377N; -.
DR   IntAct; O25614; 4.
DR   MINT; O25614; -.
DR   STRING; 85962.HP_0961; -.
DR   PaxDb; 85962-C694_04950; -.
DR   EnsemblBacteria; AAD08003; AAD08003; HP_0961.
DR   KEGG; hpy:HP_0961; -.
DR   PATRIC; fig|85962.47.peg.1029; -.
DR   eggNOG; COG0240; Bacteria.
DR   InParanoid; O25614; -.
DR   OrthoDB; 9812273at2; -.
DR   PhylomeDB; O25614; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IBA:GO_Central.
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:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome.
FT   CHAIN           1..312
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]"
FT                   /id="PRO_0000137971"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         241..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
FT   BINDING         267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00394"
SQ   SEQUENCE   312 AA;  33392 MW;  5786864D43E8D266 CRC64;
     MEIAVFGGGA WGRALAFAFG EKNEVKIISR RDLNEPLKKL NDALISKGSA PIEQVDLQRG
     LKATLYVIAI SVQHLREWFQ NASLPKNAKV LIASKGIEVL NKAFVSEIAK DFIDPNSLCF
     LAGPSFAAEI IQGLPCALVI HSNNQALALE FANKTPSFIR AYAQQDIIGG EIAGAYKNVI
     AIAGGVCDGL KLGNSAKASL LSRGLVEMQR FGAFFGGKTE TFLGLSGAGD LFLTANSILS
     RNYRVGLGLA QNKPLEVVLE ELGEVAEGVK TTNAIVEIAR KYGIYTPIAS ELALLLKGKS
     VLESMNDLIR RA
//