CDPAS_THEAC
ID CDPAS_THEAC Reviewed; 176 AA.
AC Q9HLW7;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Ta0107;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445063; CAC11255.1; -; Genomic_DNA.
DR RefSeq; WP_010900534.1; NC_002578.1.
DR AlphaFoldDB; Q9HLW7; -.
DR SMR; Q9HLW7; -.
DR STRING; 273075.Ta0107; -.
DR EnsemblBacteria; CAC11255; CAC11255; CAC11255.
DR GeneID; 1455761; -.
DR KEGG; tac:Ta0107; -.
DR eggNOG; arCOG04106; Archaea.
DR HOGENOM; CLU_105710_0_0_2; -.
DR OMA; GKTWRGT; -.
DR OrthoDB; 124973at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001024; 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..176
FT /note="CDP-archaeol synthase"
FT /id="PRO_0000094182"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ SEQUENCE 176 AA; 19399 MW; 1F9DD4CF6B1542A9 CRC64;
MQSIILFIPA LIANSGAVIT GGHFIIDRGK KFIDGRRILG NGKTLSGYAG GIAIGTVTGF
IIYLISTLFN YALGTYGTLA EAIIIPFIMA TGSLTGDIAG SFVKRRIGID RGGKGGLLDQ
WPFALMAFLF LYIFERPFFM YHYFYVTMIV ILVIVPPIHR AVNIIGYKMH KKDVPW
