ID H1KWJ9_9EURY Unreviewed; 179 AA. AC H1KWJ9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 22-FEB-2023, entry version 39. DE RecName: Full=CDP-archaeol synthase {ECO:0000256|HAMAP-Rule:MF_01117}; DE EC=2.7.7.67 {ECO:0000256|HAMAP-Rule:MF_01117}; DE AltName: Full=CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase {ECO:0000256|HAMAP-Rule:MF_01117}; GN Name=carS {ECO:0000256|HAMAP-Rule:MF_01117}; GN ORFNames=MetfoDRAFT_0172 {ECO:0000313|EMBL:EHP89576.1}; OS Methanotorris formicicus Mc-S-70. OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanotorris. OX NCBI_TaxID=647171 {ECO:0000313|EMBL:EHP89576.1, ECO:0000313|Proteomes:UP000003706}; RN [1] {ECO:0000313|EMBL:EHP89576.1, ECO:0000313|Proteomes:UP000003706} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mc-S-70 {ECO:0000313|EMBL:EHP89576.1, RC ECO:0000313|Proteomes:UP000003706}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Sieprawska-Lupa M., Takai K., Miyazaki J., RA Whitman W., Woyke T.J.; RT "The draft genome of Methanotorris formicicus Mc-S-70."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn- CC glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1- CC phosphate (DGGGP) and CTP. This reaction is the third ether-bond- CC formation step in the biosynthesis of archaeal membrane lipids. CC {ECO:0000256|HAMAP-Rule:MF_01117}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + CC H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate; CC Xref=Rhea:RHEA:25690, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58837, ChEBI:CHEBI:58838; EC=2.7.7.67; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01117}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01117}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. CC {ECO:0000256|HAMAP-Rule:MF_01117}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01117}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01117}. CC -!- SIMILARITY: Belongs to the CDP-archaeol synthase family. CC {ECO:0000256|HAMAP-Rule:MF_01117}. 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:EHP89576.1}. 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; AGJL01000002; EHP89576.1; -; Genomic_DNA. DR RefSeq; WP_007043618.1; NZ_AGJL01000002.1. DR AlphaFoldDB; H1KWJ9; -. DR STRING; 647171.MetfoDRAFT_0172; -. DR EnsemblBacteria; EHP89576; EHP89576; MetfoDRAFT_0172. DR PATRIC; fig|647171.4.peg.171; -. DR OrthoDB; 45383at2157; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000003706; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043338; F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_01117; CDP_archaeol_synth; 1. DR InterPro; IPR032690; CarS. DR InterPro; IPR002726; CarS_archaea. DR PANTHER; PTHR39650; CDP-ARCHAEOL SYNTHASE; 1. DR PANTHER; PTHR39650:SF1; CDP-ARCHAEOL SYNTHASE; 1. DR Pfam; PF01864; CarS-like; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01117}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01117}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01117}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01117}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01117}; KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01117}; KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01117}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01117}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01117}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01117}. FT TRANSMEM 6..29 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01117" FT TRANSMEM 50..72 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01117" FT TRANSMEM 84..105 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01117" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01117" SQ SEQUENCE 179 AA; 19704 MW; 3E7D148731554E47 CRC64; MDIVGLVFSS FWYILPAYIA NATACIFGGG TPLDLGRNFI DGRRLIGNGV TFRGTFSGIL CGTIAAILQG VILNLKIINT PMVFYSNIFE CAFLGFLLSS GALFGDMVGS FIKRRLEIKQ GNPAPILDQL NFVFGAILFT YPFSPLPLNM IITICVITPI IHLTSNIIAY KLKIKKVWW //