ID C5QSL7_9STAP Unreviewed; 332 AA. AC C5QSL7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 02-OCT-2024, entry version 84. 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)(+)-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394}; DE AltName: Full=NAD(P)H-dependent dihydroxyacetone-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394, GN ECO:0000313|EMBL:EES40120.1}; GN ORFNames=HMPREF0793_2223 {ECO:0000313|EMBL:EES40120.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES40120.1, ECO:0000313|Proteomes:UP000003152}; RN [1] {ECO:0000313|EMBL:EES40120.1, ECO:0000313|Proteomes:UP000003152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES40120.1, RC ECO:0000313|Proteomes:UP000003152}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L., RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reduction of the glycolytic intermediate CC dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the CC key precursor for phospholipid synthesis. {ECO:0000256|HAMAP- CC Rule:MF_00394}. 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00394}. 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:EES40120.1}. 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; ACJB01000063; EES40120.1; -; Genomic_DNA. DR RefSeq; WP_002442972.1; NZ_GG696773.1. DR AlphaFoldDB; C5QSL7; -. DR GeneID; 58051172; -. DR eggNOG; COG0240; Bacteria. DR HOGENOM; CLU_033449_0_2_9; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000003152; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0141153; F:glycerol-3-phosphate dehydrogenase (NADP+) activity; IEA:RHEA. 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:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. 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-UniRule. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. 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 NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00394}; KW Nucleotide-binding {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..160 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|PIRSR:PIRSR000114-3" FT BINDING 11 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 12 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 32 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 49 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 106 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 106 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 106 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 137 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 139 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 141 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 141 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 192 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 245 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 255 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 256..257 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 256 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 256 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 256 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 257 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 280 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 282 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" SQ SEQUENCE 332 AA; 36070 MW; 7A7022EB471E869F CRC64; MTKITVFGMG SFGTALANVL AQNGHDVLMW GKNNDSVEEL NTHHMNKNYL KEAKLEESIQ ATTDLKQATQ FSDIFLMALP TKAMREVASN IDEMLESKKT FIHVAKGIEN GTFKRVSEML EDSISPEHNA GIGVLSGPSH AEEVVIKQPT TVAASSKDKK ISALIQDLFM NDYLRVYTNN DLVGVELGGA LKNIIAVASG IVAGMGFGDN AKAALMTRGL AEISRLGEKL GADPMTFLGL GGIGDLIVTC TSTHSRNFTL GYKLGQGKTM DDALKEMNMV VEGVYTTKSV YHLAKEENVD MPITSALYRV LFEDIPVKDS VKELMGRDKK AE //