CDPAS_METST
ID CDPAS_METST Reviewed; 187 AA.
AC Q2NHB7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Msp_0385;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC56786.1; -; Genomic_DNA.
DR RefSeq; WP_011405986.1; NC_007681.1.
DR AlphaFoldDB; Q2NHB7; -.
DR SMR; Q2NHB7; -.
DR STRING; 339860.Msp_0385; -.
DR EnsemblBacteria; ABC56786; ABC56786; Msp_0385.
DR GeneID; 41324959; -.
DR KEGG; mst:Msp_0385; -.
DR eggNOG; arCOG04106; Archaea.
DR HOGENOM; CLU_105710_0_0_2; -.
DR OMA; GKTWRGT; -.
DR OrthoDB; 124973at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001931; 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..187
FT /note="CDP-archaeol synthase"
FT /id="PRO_0000298281"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ SEQUENCE 187 AA; 20445 MW; 4BDB0F4858824180 CRC64;
MDILTLIFYS IYLMIPAYLA NGSALVFGGG TPMDFGHYCW DNRRLIGNGV TWRGTVCGGL
FGMVIGGILG LLATYGIGSY FFNITASQIT FMSGFVPQGL LVGFLLGFGA LIGDAIGSFL
KRRLNFERGK PVPLLDQLDF VVVSLLFVST VVSLSLEMIV IIILVSIFLH LGANMFAYMI
NLKDVWY
