CDPAS_NATPD
ID CDPAS_NATPD Reviewed; 189 AA.
AC Q3ITE8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=NP_0990A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48586.1; -; Genomic_DNA.
DR RefSeq; WP_011322221.1; NC_007426.1.
DR AlphaFoldDB; Q3ITE8; -.
DR SMR; Q3ITE8; -.
DR STRING; 348780.NP_0990A; -.
DR EnsemblBacteria; CAI48586; CAI48586; NP_0990A.
DR GeneID; 3702595; -.
DR KEGG; nph:NP_0990A; -.
DR eggNOG; arCOG04106; Archaea.
DR HOGENOM; CLU_105710_0_0_2; -.
DR OMA; GKTWRGT; -.
DR OrthoDB; 124973at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000002698; 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..189
FT /note="CDP-archaeol synthase"
FT /id="PRO_0000298283"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ SEQUENCE 189 AA; 19794 MW; C1937BC86CF5DFC9 CRC64;
MVAETVAIAV WAMLPAYVPN NVAVLAGGGR PIDGGRTLDK LTDEDGVLYD ENRILGDGKT
WRGTAFGTAA GVVLALLLNQ LQPFVAGTVG VPQFPIAAAV ALAFGAMLGD ILASFLKRRT
GRQRGAAFPG VDQLDFVIVS LALTAIVATG WFLATFTLPV LVAIFVLTPV LHVSTNGLAY
AFGLKDEPW
