ID A0A5C7ENU9_9ACTN Unreviewed; 335 AA. AC A0A5C7ENU9; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 24-JUL-2024, entry version 16. 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 ORFNames=E4J93_04470 {ECO:0000313|EMBL:TXF36661.1}; OS Collinsella sp. BA40. OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella. OX NCBI_TaxID=2560852 {ECO:0000313|EMBL:TXF36661.1, ECO:0000313|Proteomes:UP000321063}; RN [1] {ECO:0000313|EMBL:TXF36661.1, ECO:0000313|Proteomes:UP000321063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA40 {ECO:0000313|EMBL:TXF36661.1, RC ECO:0000313|Proteomes:UP000321063}; RA Park J.-K.; RT "Collinsella canisensis sp. nov., a novel bacterium isolated from canine RT feces."; RL Submitted (AUG-2019) 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:TXF36661.1}. 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; VOWY01000010; TXF36661.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5C7ENU9; -. DR OrthoDB; 9812273at2; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000321063; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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: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:0046474; P:glycerophospholipid biosynthetic process; IEA:TreeGrafter. DR GO; GO:0006116; P:NADH oxidation; IEA:TreeGrafter. 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. 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 NADP {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:UP000321063}. FT DOMAIN 2..157 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 178..318 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 189 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|PIRSR:PIRSR000114-3" FT BINDING 10 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 11 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 31 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 48 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 105 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 105 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 105 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 134 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 138 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 138 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 189 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 242 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 252 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 253..254 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 253 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 253 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 253 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 254 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 277 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 279 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" SQ SEQUENCE 335 AA; 34861 MW; 4882E5C9424388FD CRC64; MKIALIGSGS WGTAVAGLAA AHADSVVMWA HGDETARGIN EHGRNPRYLS DYELPANIAA TASIQEALKG ADGVVFAVPS AHLRSVAHDA ADFMDSATPV LCLTKGVEPG TGLLMSEVIA DEIGHPERIA ALSGPNHAEE ICRGGLSAAV IASEDPAISD FFKRLLITQA FRIYVSHDMV GVETCGAMKN IIAIVCGISA GAGYGDNTLA LIMTRGLAEI SRVVSARGGD PITCMGLAGM GDLVATCTSE HSRNRSFGVA FSHGVSLDEY QDSSHMVVEG AAAAISVAEL ADRLGVEVPL TSVLNRTLFH GGTIAEALEL LTDRCPTQEF YGIDD //