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CDPAS_PYRAB
ID   CDPAS_PYRAB             Reviewed;         168 AA.
AC   Q9UY86; G8ZJX6;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   25-MAY-2022, entry version 99.
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=PYRAB16220;
GN   ORFNames=PAB1285;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB50526.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248288; CAB50526.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE71083.1; -; Genomic_DNA.
DR   PIR; H75010; H75010.
DR   RefSeq; WP_048147117.1; NC_000868.1.
DR   AlphaFoldDB; Q9UY86; -.
DR   SMR; Q9UY86; -.
DR   STRING; 272844.PAB1285; -.
DR   EnsemblBacteria; CAB50526; CAB50526; PAB1285.
DR   GeneID; 1495912; -.
DR   KEGG; pab:PAB1285; -.
DR   PATRIC; fig|272844.11.peg.1732; -.
DR   eggNOG; arCOG04106; Archaea.
DR   HOGENOM; CLU_105710_0_0_2; -.
DR   OrthoDB; 124973at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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..168
FT                   /note="CDP-archaeol synthase"
FT                   /id="PRO_0000094174"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        112..132
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   168 AA;  18708 MW;  28A49F58A9018AE9 CRC64;
     MNPIFEAFWY ILPAYFANSS PVVLGGGTPI DFGKKWRDGR RIFGDGKTWR GFFGGITVGT
     VVGTIQHLMF PGYYGSLKLA VGVAFLLSLG ALVGDLIGSF IKRRLNMPRG YPAVGLDQWG
     FLISALCFAY PLRTIPTGEV LFLLVVTPVI HWLANVFAYR MKWKNVPW
 
 
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