ID C7MY23_SACVD Unreviewed; 336 AA. AC C7MY23; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 02-SEP-2026, entry version 99. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|ARBA:ARBA00069372, ECO:0000256|HAMAP-Rule:MF_00394}; DE EC=1.1.1.94 {ECO:0000256|ARBA:ARBA00066687, 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|ARBA:ARBA00080511, ECO:0000256|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394}; GN OrderedLocusNames=Svir_09130 {ECO:0000313|EMBL:ACU95971.1}; OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / CCUG OS 5913 / NBRC 12207 / NCIMB 9602 / P101) (Thermoactinomyces viridis). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU95971.1, ECO:0000313|Proteomes:UP000000841}; RN [1] {ECO:0000313|EMBL:ACU95971.1, ECO:0000313|Proteomes:UP000000841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101 RC {ECO:0000313|Proteomes:UP000000841}; RX PubMed=21304650; DOI=10.4056/sigs.20263; RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D., RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N., RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Saccharomonospora viridis type strain RT (P101)."; RL Stand. Genomic Sci. 1:141-149(2009). 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=sn-glycerol 3-phosphate + NAD(+) = dihydroxyacetone phosphate CC + NADH + H(+); 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=sn-glycerol 3-phosphate + NADP(+) = dihydroxyacetone phosphate CC + NADPH + H(+); 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; CC Evidence={ECO:0000256|ARBA:ARBA00052716}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11098; CC Evidence={ECO:0000256|ARBA:ARBA00052716}; 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 --------------------------------------------------------------------------- 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; CP001683; ACU95971.1; -; Genomic_DNA. DR RefSeq; WP_012796400.1; NC_013159.1. DR AlphaFoldDB; C7MY23; -. DR STRING; 471857.Svir_09130; -. DR KEGG; svi:Svir_09130; -. DR eggNOG; COG0240; Bacteria. DR HOGENOM; CLU_033449_0_2_11; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000841; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0141152; F:glycerol-3-phosphate dehydrogenase (NAD+) activity; IEA:RHEA. DR GO; GO:0141153; F:glycerol-3-phosphate dehydrogenase (NADP+) activity; IEA:RHEA. 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-UniRule. DR FunFam; 1.10.1040.10:FF:000001; Glycerol-3-phosphate dehydrogenase [NAD(P)+]; 1. DR FunFam; 3.40.50.720:FF:000019; Glycerol-3-phosphate dehydrogenase [NAD(P)+]; 1. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1. 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 NCBIfam; NF000940; PRK00094.1-2; 1. DR NCBIfam; NF000942; PRK00094.1-4; 1. 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}; Reference proteome {ECO:0000313|Proteomes:UP000000841}. FT DOMAIN 6..161 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 182..320 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 193 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 13 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 14 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 34 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 35 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 51 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 108 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 108 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 138 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 142 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 142 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 193 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 246 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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..258 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 257 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 257 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" 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 258 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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" FT BINDING 284 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" SQ SEQUENCE 336 AA; 35337 MW; 14A3033E7C3ECACE CRC64; MSVQRVTVLG AGSWGTTFAK VLADAGRDVT LWARRAEVAD EIRTQHTNSS YLPGVRLPER LTATSDAATA LEAADAVVFA VPSQKLRENL AAWRDLLPAD AILVSLAKGV ELGTLKRMSE VISDITGVEP GDVVVVSGPN LAKEIAQQQP AAAVLACADH DRAVAIQQAS FNSYFRPYTN TDVVGCELGG ACKNVIALSC GMAAGLGYGT NTMATLITRG LAEMARLGAA LGADPLTFAG LAGVGDLVAT CSSPLSRNRT FGERIGRGET MEQARAAQGG QVAEGVTSCR SIRELARRLD VDMPITDAMY RVCHEGVDPG TVGAELLGRR QKHEWS //