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CDSA_RICPR
ID   CDSA_RICPR              Reviewed;         228 AA.
AC   Q9ZDA8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Phosphatidate cytidylyltransferase;
DE            EC=2.7.7.41;
DE   AltName: Full=CDP-DAG synthase;
DE   AltName: Full=CDP-DG synthase;
DE   AltName: Full=CDP-diacylglycerol synthase;
DE            Short=CDS;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase;
DE   AltName: Full=CDP-diglyceride synthase;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN   Name=cdsA; OrderedLocusNames=RP424;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC         diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; AJ235271; CAA14881.1; -; Genomic_DNA.
DR   PIR; G71700; G71700.
DR   RefSeq; NP_220805.1; NC_000963.1.
DR   RefSeq; WP_010886291.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDA8; -.
DR   SMR; Q9ZDA8; -.
DR   STRING; 272947.RP424; -.
DR   EnsemblBacteria; CAA14881; CAA14881; CAA14881.
DR   GeneID; 57569549; -.
DR   KEGG; rpr:RP424; -.
DR   PATRIC; fig|272947.5.peg.437; -.
DR   eggNOG; COG0575; Bacteria.
DR   HOGENOM; CLU_037294_1_1_5; -.
DR   OMA; LIMLYFC; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR000374; PC_trans.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..228
FT                   /note="Phosphatidate cytidylyltransferase"
FT                   /id="PRO_0000090745"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   228 AA;  25814 MW;  48DE66AB6EA19174 CRC64;
     MITQKEKEHL AKDKQNIYLR IISGIALVSL FVIAILCLKT LFYILMILVG LGMLSEWYNM
     TYPSINYLLI GLIIIPIPIS LLIFLSMEES NRLVIMLYFC ILWSVDTFAM IGGKTFKGIK
     LAPKISPKKT WTGLITGTVS AGLVSVLVSL IPNYHIEHYY FSNKIYLFII SCILALIAQS
     SDLFISYFKR KFNIKDSGHI IPGHGGVLDR FDSIILTAPV FFCINIYL
 
 
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