ID G1PDH_THESM Reviewed; 350 AA. AC C6A2E4; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 29-SEP-2021, entry version 69. 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}; OrderedLocusNames=TSIB_0726; OS Thermococcus sibiricus (strain DSM 12597 / MM 739). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=604354; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12597 / MM 739; RX PubMed=19447963; DOI=10.1128/aem.00718-09; RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.; RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome RT analysis."; RL Appl. Environ. Microbiol. 75:4580-4588(2009). 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=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate CC + H(+) + NADH; 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=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate CC + H(+) + NADPH; 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; CC Evidence={ECO:0000255|HAMAP-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 -!- 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; CP001463; ACS89789.1; -; Genomic_DNA. DR SMR; C6A2E4; -. DR STRING; 604354.TSIB_0726; -. DR EnsemblBacteria; ACS89789; ACS89789; TSIB_0726. DR KEGG; tsi:TSIB_0726; -. DR eggNOG; arCOG00982; Archaea. DR HOGENOM; CLU_038362_0_0_2; -. DR OMA; AEHLFSH; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000009079; 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:UniProtKB-KW. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1. DR InterPro; IPR023002; G1P_dehydrogenase_arc. DR InterPro; IPR032837; G1PDH. DR InterPro; IPR016205; Glycerol_DH. DR PANTHER; PTHR43616; PTHR43616; 1. DR Pfam; PF13685; Fe-ADH_2; 1. DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 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..350 FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]" FT /id="PRO_1000206482" FT NP_BIND 97..101 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT NP_BIND 119..122 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT METAL 171 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT METAL 251 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT METAL 267 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 124 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 128 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 171 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" FT BINDING 255 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00497" SQ SEQUENCE 350 AA; 38069 MW; 74DD6AA862A25B71 CRC64; MVMFMHLMEL PREVLLGEDL KDKVSQVAKR LKLGENVLIL YGPKTKEIAG KDIEKHLKEF FHVKNLLIKE ASMKNVQKAL EIIRNENIDW LLGVGGGSII DVAKLASFKA DVPFISFPTT ASHDGIASAN ASIRDLGAKT SIKARPPVAV IADVNIIKTA PYRYLAAGVG DMVSNLTAVK DWELAHRIRG EYFSEYAASL SLMSAKMVIK NADIIRLSNE ESVRKVIKAL ISSGVAMSIA GSSRPASGAE HLFSHALDAI APKPALHGEQ CGVGTIIMAY LHGLNWKKIR ETLKRVGAPT NAYELEIDPG FIIEALTIAH TIRPERYTIL GKDGLTKEAA EKAAKITGVI //