ID   CDPAS_METAR             Reviewed;         174 AA.
AC   Q0W6Q1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=CDP-archaeol synthase {ECO:0000255|HAMAP-Rule:MF_01117};
DE            EC=2.7.7.67 {ECO:0000255|HAMAP-Rule:MF_01117};
DE   AltName: Full=CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase {ECO:0000255|HAMAP-Rule:MF_01117};
GN   Name=carS {ECO:0000255|HAMAP-Rule:MF_01117}; OrderedLocusNames=UNCMA_22430;
GN   ORFNames=RCIX520;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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:0000255|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:0000255|HAMAP-Rule:MF_01117};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01117};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01117};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- SIMILARITY: Belongs to the CDP-archaeol synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
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DR   EMBL; AM114193; CAJ35942.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0W6Q1; -.
DR   SMR; Q0W6Q1; -.
DR   STRING; 351160.RCIX520; -.
DR   EnsemblBacteria; CAJ35942; CAJ35942; RCIX520.
DR   KEGG; rci:RCIX520; -.
DR   eggNOG; arCOG04106; Archaea.
DR   OMA; GKTWRGT; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000663; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; PTHR39650; 1.
DR   Pfam; PF01864; CarS-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..174
FT                   /note="CDP-archaeol synthase"
FT                   /id="PRO_0000298290"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ   SEQUENCE   174 AA;  18956 MW;  E60CEBE58AB4E88A CRC64;
     MIPAGLANPF AALFGGGTPI DFGKNFKDNR RILGDGKTYR GLIFGSLCGT LIGLLQILLA
     PHIAPYLAGF IDPSLLVGYS YIALITMPFG ALLGDIVKSF FKRRLGFERG AMLPIADQLD
     FVAGAWVLTF LLDPEWLLAN FTIWVAIAVI LIIPVFHVAF NIAGYKLGKK DVPW