ID G1PDH_SULAC Reviewed; 351 AA. AC Q4JB01; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 2. DT 04-NOV-2026, entry version 103. 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=Saci_0640; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). 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 -!- SEQUENCE CAUTION: CC Sequence=AAY80028.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000077; AAY80028.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_015385466.1; NC_007181.1. DR AlphaFoldDB; Q4JB01; -. DR SMR; Q4JB01; -. DR STRING; 330779.Saci_0640; -. DR GeneID; 14551162; -. DR KEGG; sai:Saci_0640; -. DR PATRIC; fig|330779.12.peg.615; -. DR eggNOG; arCOG00982; Archaea. DR HOGENOM; CLU_038362_0_0_2; -. DR OMA; AACHLYI; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000001018; 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..351 FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]" FT /id="PRO_0000157352" 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 351 AA; 38584 MW; 307FAC9F0BC9B20B CRC64; MEIKEHIINL PKHIYTGYGI LDNFRNYLQT LNLPQPFLVI TGPVIHQEIF SKRIEEHIKD FKYEVVIVNK SDLSEAEKVE DIARQKGIKT ILGVGGGTVI DIAKFTAYKI DREFISIPTS PSHDGITSPF AAIKGLGKPI SIKAKEPLAI ISDVEILASA PRRLINAGIG DTLGKITAVR DWRLAHKLRG EYYGDYTASL ALMSARHALS CTKIINKDIR AGVRVLTEAL ISSGVAMGMA GSTRPASGSE HLFAHAIELL YPNLGLHGEL VALGTIMMAY IHGINWRRIR RAMKKIGLPV TSKQIGIPDE GIIKALTIAH SIRPERYTIL GDRGLTWESA EKIARETGVI S //