GPDA_HELPS
ID GPDA_HELPS Reviewed; 312 AA.
AC B2UUA7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=HPSH_05065;
OS Helicobacter pylori (strain Shi470).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=512562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shi470;
RA Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT Asian ancestry of the first Americans.";
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}.
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DR EMBL; CP001072; ACD48439.1; -; Genomic_DNA.
DR RefSeq; WP_000401716.1; NC_010698.2.
DR AlphaFoldDB; B2UUA7; -.
DR SMR; B2UUA7; -.
DR KEGG; hps:HPSH_05065; -.
DR HOGENOM; CLU_033449_0_2_7; -.
DR OMA; LATCNSP; -.
DR UniPathway; UPA00940; -.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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: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;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism.
FT CHAIN 1..312
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_1000190158"
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; 33418 MW; EBAD1DF0864630DB CRC64;
MEIAVFGGGA WGRALAFAFG EKNEVKIISR RDLNEPLKKL NDALISKGSA PIEQVDLQRG
LKAVLYVIAI SVQHLREWFQ NASLPKNAKV LIASKGIEVL NRAFVSEIAK DFIDPNSLCF
LAGPSFAAEI IQGLPCALVI HSNNQALALE FANKTPSFIR AYAQQDIIGG EIAGAYKNVI
AIAGGVCDGL KLGNSAKASL LSRGLVEMQR FGAFFGGKTE TFLGLSGAGD LFLTANSILS
RNYRVGLGLA QNKPLEVVLE ELGEVAEGVK TTNAIVEIAR KYGIYTPIAS ELALLLKGKS
VLESMNDLIR RA
