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Database: UniProt
Entry: K2L243_HELPX
LinkDB: K2L243_HELPX
Original site: K2L243_HELPX 
ID   K2L243_HELPX            Unreviewed;       312 AA.
AC   K2L243;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
DE            EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
GN   Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394};
GN   ORFNames=OUK_1252 {ECO:0000313|EMBL:EKE88729.1};
OS   Helicobacter pylori R037c.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1145114 {ECO:0000313|EMBL:EKE88729.1, ECO:0000313|Proteomes:UP000006760};
RN   [1] {ECO:0000313|EMBL:EKE88729.1, ECO:0000313|Proteomes:UP000006760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R037c {ECO:0000313|EMBL:EKE88729.1,
RC   ECO:0000313|Proteomes:UP000006760};
RX   PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA   Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA   Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA   Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT   "Genome sequences of 65 Helicobacter pylori strains isolated from
RT   asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT   disease, or gastritis.";
RL   Pathog. Dis. 68:39-43(2013).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00394, ECO:0000256|RuleBase:RU000439};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00394}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC       ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKE88729.1}.
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DR   EMBL; AMOU01000006; EKE88729.1; -; Genomic_DNA.
DR   RefSeq; WP_000401683.1; NZ_AMOU01000006.1.
DR   AlphaFoldDB; K2L243; -.
DR   PATRIC; fig|1145114.3.peg.1223; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000006760; Unassembled WGS sequence.
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-UniRule.
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; 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 {ECO:0000256|HAMAP-Rule:MF_00394};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00394};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00394};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00394};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|HAMAP-Rule:MF_00394};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW   Rule:MF_00394}.
FT   DOMAIN          2..147
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          166..301
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT                   ECO:0000256|PIRSR:PIRSR000114-1"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT                   ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT                   ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT                   ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         241..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT                   ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT                   ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
SQ   SEQUENCE   312 AA;  33393 MW;  F25E1C748E50089F CRC64;
     MEIAVFGGGA WGRALAFAFG EKNEVKIISR RDLNEPLKKL NDALISKGSA PIEQVDLEKG
     LKAALYVIAI SVQHLREWFQ NASLPKNAKV LIASKGIEVL NRAFVSEIAK DFIDPNSLCF
     LAGPSFAAEI IQGLPCALVI HSNNQALALE FANKTPSFIR AYAQQDIIGG EIAGAYKNVI
     AIAGGVCDGL KLGNSAKASL LSRGLVEMQR FGAFFGGKTE TFLGLSGAGD LFLTANSILS
     RNYRVGLGLA QNKPLEVVLE ELGEVAEGVK TTNAIVEIAR KYGIYTPIAS ELALLLKGKS
     VLESMNDLIR RT
//
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