ID C3GGH7_BACTU Unreviewed; 340 AA.
AC C3GGH7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 79.
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=bthur0010_13510 {ECO:0000313|EMBL:EEM78579.1};
OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM78579.1};
RN [1] {ECO:0000313|EMBL:EEM78579.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM78579.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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:EEM78579.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACNH01000031; EEM78579.1; -; Genomic_DNA.
DR RefSeq; WP_000161776.1; NZ_CM000755.1.
DR AlphaFoldDB; C3GGH7; -.
DR SMR; C3GGH7; -.
DR HOGENOM; CLU_033449_0_2_9; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000006660; Chromosome.
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|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00394};
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 3..161
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 181..321
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 8..13
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 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 141
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 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 256
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 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
SQ SEQUENCE 340 AA; 36593 MW; C9F726A6F3465B45 CRC64;
MTKITVVGAG SWGTALAMVL ADNGHDVRIW GNRSELMDEI NTKHENSRYL PGITLPSTIV
AYSSLEEALV DVNVVLLVVP TKAYREVLQD MKKYVAGPTT WIHASKGIEP GTSKRISEVI
EEEIPEDLIK DVVVLSGPSH AEEVGLRQAT TVTSAAKRME AAEEVQDLFM NSYFRVYTNP
DIVGVELGGA LKNIIALAAG ITDGLGLGDN AKAALMTRGL TEIARLGRKM GGNPLTFAGL
TGMGDLIVTC TSVHSRNWRA GNMLGKGHSL EEVLESMGMV VEGVRTTKAA HELAEKMEVE
MPITAALYDV LFNGNNVKDA VGSLMGRVRK HEVEAIPDLL
//
