CDPAS_PYRFU
ID CDPAS_PYRFU Reviewed; 167 AA.
AC Q8U3Q8;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=PF0398;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL80522.1; -; Genomic_DNA.
DR RefSeq; WP_011011511.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U3Q8; -.
DR SMR; Q8U3Q8; -.
DR STRING; 186497.PF0398; -.
DR EnsemblBacteria; AAL80522; AAL80522; PF0398.
DR GeneID; 41712195; -.
DR KEGG; pfu:PF0398; -.
DR PATRIC; fig|186497.12.peg.413; -.
DR eggNOG; arCOG04106; Archaea.
DR HOGENOM; CLU_105710_0_0_2; -.
DR OMA; GKTWRGT; -.
DR OrthoDB; 124973at2157; -.
DR PhylomeDB; Q8U3Q8; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001013; 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..167
FT /note="CDP-archaeol synthase"
FT /id="PRO_0000094176"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ SEQUENCE 167 AA; 18511 MW; 3714383D9C47DD29 CRC64;
MHPILEAFWY ILPAYFANSS PVILGGGTPI DFGKTWRDGR RIFGDSKTWR GFLGGLTVGT
LIGVIQQIIY PYYPSLSLAF KVSFLLALGA LVGDLIGSFI KRRLNLPPGY PAVGLDQWGF
LISALCFAYP VHTIPTGEVL LLLVVTPLIH WGTNVLAYKM KWKSVPW
