ID   CDPAS_AERPE             Reviewed;         174 AA.
AC   Q9YF05;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=APE_0433;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(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; BA000002; BAA79391.1; -; Genomic_DNA.
DR   PIR; C72737; C72737.
DR   PDB; 5GUF; X-ray; 2.40 A; A=1-174.
DR   PDBsum; 5GUF; -.
DR   AlphaFoldDB; Q9YF05; -.
DR   SMR; Q9YF05; -.
DR   STRING; 272557.APE_0433; -.
DR   EnsemblBacteria; BAA79391; BAA79391; APE_0433.
DR   KEGG; ape:APE_0433; -.
DR   eggNOG; arCOG04106; Archaea.
DR   OMA; GKTWRGT; -.
DR   BRENDA; 2.7.7.67; 171.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000002518; 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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Magnesium; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..174
FT                   /note="CDP-archaeol synthase"
FT                   /id="PRO_0000094166"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        59..79
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        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   HELIX           14..29
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   HELIX           31..34
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   TURN            40..43
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   HELIX           59..80
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   HELIX           84..109
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   HELIX           121..136
FT                   /evidence="ECO:0007829|PDB:5GUF"
FT   HELIX           143..161
FT                   /evidence="ECO:0007829|PDB:5GUF"
SQ   SEQUENCE   174 AA;  17953 MW;  BD4C321CB0979DBE CRC64;
     MALELAVDWR IDNILEAIIL MLPAMIANAT PVVAGGRRPV DMGVVLPDGR RLLGDGKTIE
     GLLAGFAAGS AAGVLAALAS GNMLLAVHSP AIALGALAGD MAGSFVKRRL GIERGRPAPL
     LDQLDFYLGA LAVSIALGYT WTPRVAVEAA AAVLLLHLAA NITAYLLGLK KVPW