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CDSA_PSEAE
ID   CDSA_PSEAE              Reviewed;         271 AA.
AC   Q59640;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 125.
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; Synonyms=cds; OrderedLocusNames=PA3651;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=8654980; DOI=10.1016/0378-1119(96)00009-1;
RA   Taguchi K., Fukutomi H., Kuroda A., Kato J., Ohtake H.;
RT   "Cloning of the Pseudomonas aeruginosa gene encoding CDP-diglyceride
RT   synthetase.";
RL   Gene 172:165-166(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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 inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; D50811; BAA09437.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG07039.1; -; Genomic_DNA.
DR   PIR; F83188; F83188.
DR   PIR; JC4832; JC4832.
DR   RefSeq; NP_252341.1; NC_002516.2.
DR   RefSeq; WP_003092388.1; NZ_QZGE01000001.1.
DR   AlphaFoldDB; Q59640; -.
DR   SMR; Q59640; -.
DR   STRING; 287.DR97_4288; -.
DR   PaxDb; Q59640; -.
DR   PRIDE; Q59640; -.
DR   DNASU; 880465; -.
DR   EnsemblBacteria; AAG07039; AAG07039; PA3651.
DR   GeneID; 880465; -.
DR   KEGG; pae:PA3651; -.
DR   PATRIC; fig|208964.12.peg.3820; -.
DR   PseudoCAP; PA3651; -.
DR   HOGENOM; CLU_037294_1_2_6; -.
DR   InParanoid; Q59640; -.
DR   OMA; WEWGRLN; -.
DR   PhylomeDB; Q59640; -.
DR   BioCyc; PAER208964:G1FZ6-3721-MON; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR000374; PC_trans.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Nucleotidyltransferase; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..271
FT                   /note="Phosphatidate cytidylyltransferase"
FT                   /id="PRO_0000090744"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        131..133
FT                   /note="WPL -> VAA (in Ref. 1; BAA09437)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  28856 MW;  5025059C3F1A64C7 CRC64;
     MLKQRIITAL VLLPIALGGF FLLEGAFFAL FIGAVVSLGA WEWARLAGYE QQFGRVAYAA
     TVAVLMVALY HLPQLAGAVL LLALVWWTLA TVLVLTYPES VGYWGGRWRR LGMGLLILLP
     AWQGLVLLKQ WPLANGLIIA VMVLVWGADI GAYFSGKAFG KRKLAPRVSP GKSWEGVYGG
     LAASLAITLA VGLYRGWSLG ALLLALLGAA LVVFVSIVGD LTESMFKRQS GIKDSSNLLP
     GHGGVLDRID SLTAAIPVFA ALLWAAGWGA P
 
 
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