CDPAS_PYRHO
ID CDPAS_PYRHO Reviewed; 170 AA.
AC O58081;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=PH0343;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29417.1; -; Genomic_DNA.
DR PIR; D71141; D71141.
DR AlphaFoldDB; O58081; -.
DR SMR; O58081; -.
DR STRING; 70601.3256734; -.
DR EnsemblBacteria; BAA29417; BAA29417; BAA29417.
DR KEGG; pho:PH0343; -.
DR eggNOG; arCOG04106; Archaea.
DR OMA; GKTWRGT; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000752; 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; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..170
FT /note="CDP-archaeol synthase"
FT /id="PRO_0000094177"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ SEQUENCE 170 AA; 18951 MW; 2CAAD2FEF3DECC12 CRC64;
MKMNQLLEAF WYILPAYFAN SSPVVLGGGT PIDFGKKWRD GRRILGDGKT WRGFFGGLIV
GTIIGIVQYF LLPEYYGSLG IAIELAFLLS LGTLVGDLIG SFIKRRLNMP RGYPAVGLDQ
WGFLIAALCF AYPVKTIPTG EVLFLLVITP LIHWGANIFA YKMGWKKVPW
