ID G1PDH_IGNH4 Reviewed; 352 AA. AC A8ABP9; DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 87. DE RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00497}; DE Short=G1P dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497}; DE Short=G1PDH {ECO:0000255|HAMAP-Rule:MF_00497}; DE EC=1.1.1.261 {ECO:0000255|HAMAP-Rule:MF_00497}; DE AltName: Full=Enantiomeric glycerophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00497}; DE AltName: Full=sn-glycerol-1-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497}; GN Name=egsA {ECO:0000255|HAMAP-Rule:MF_00497}; GN OrderedLocusNames=Igni_1174; OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Ignicoccus. OX NCBI_TaxID=453591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIN4/I / DSM 18386 / JCM 14125; RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158; RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A., RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C., RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A., RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H., RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.; RT "A genomic analysis of the archaeal system Ignicoccus hospitalis- RT Nanoarchaeum equitans."; RL Genome Biol. 9:R158.1-R158.18(2008). CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of CC dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1- CC phosphate (G1P). The G1P thus generated is used as the glycerophosphate CC backbone of phospholipids in the cellular membranes of Archaea. CC {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- CATALYTIC ACTIVITY: CC Reaction=sn-glycerol 1-phosphate + NAD(+) = dihydroxyacetone phosphate CC + NADH + H(+); Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, CC ChEBI:CHEBI:57945; EC=1.1.1.261; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00497}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sn-glycerol 1-phosphate + NADP(+) = dihydroxyacetone phosphate CC + NADPH + H(+); Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.1.1.261; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00497}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00497}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00497}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00497}. 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; CP000816; ABU82351.1; -; Genomic_DNA. DR RefSeq; WP_012123315.1; NC_009776.1. DR AlphaFoldDB; A8ABP9; -. DR SMR; A8ABP9; -. DR STRING; 453591.Igni_1174; -. DR GeneID; 5561731; -. DR KEGG; iho:Igni_1174; -. DR eggNOG; arCOG00982; Archaea. DR HOGENOM; CLU_038362_0_0_2; -. DR OrthoDB; 8656at2157; -. DR PhylomeDB; A8ABP9; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000262; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0106357; F:glycerol-1-phosphate dehydrogenase (NAD+) activity; IEA:RHEA. DR GO; GO:0106358; F:glycerol-1-phosphate dehydrogenase (NADP+) activity; IEA:RHEA. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd08173; Gro1PDH; 1. DR Gene3D; 3.40.50.1970; -; 1. DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1. DR HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1. DR InterPro; IPR023002; G1P_dehydrogenase_arc. DR InterPro; IPR032837; G1PDH_N. DR InterPro; IPR016205; Glycerol_DH. DR NCBIfam; NF002022; PRK00843.1; 1. DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1. DR PANTHER; PTHR43616:SF5; GLYCEROL DEHYDROGENASE 1; 1. DR Pfam; PF13685; Fe-ADH_2; 1. DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1. DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1. PE 3: Inferred from homology; KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Metal-binding; NAD; NADP; KW Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Zinc. FT CHAIN 1..352 FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]" FT /id="PRO_0000350646" FT BINDING 97..101 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 119..122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 128 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 171 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 251 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 267 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" SQ SEQUENCE 352 AA; 38031 MW; 7FD9612CC30CF2C9 CRC64; MRDRHEIELM KRVVVGRGTR RELPKVIKAL GFDGGEVLVV TGPHVWSEWG DELQGLLEKE GFKVDFVTVV EPSVEEANKV LEGLNGEPNV VVGFGGGKAI DVAKYVAMKL GRDVVSVPTA TSHDGIASPF SSLKGLKGPT SVKTKTPIAV VADIEVIARA PERLNRAGIG DVLAKFSAVR DWRLAHVLKG EYYGSYAASL ALMSAKHVLK YSPLLKALSE DGLRILVEAL ISSGVAMCIA GSSRPASGSE HLFSHALDVI ANRPALHGEQ VGVGTIMMLY LHGSKLWRKV RKVLRDLNLP TTAEELGVED EKIIEALTIA HKIRPERYTI LGSDGLTREA AERLARTTGV IK //