(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NUT1_YERPA

ID   A0A0E1NUT1_YERPA        Unreviewed;       282 AA.
AC   A0A0E1NUT1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 18.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|RuleBase:RU003938};
DE            EC=2.7.7.41 {ECO:0000256|RuleBase:RU003938};
DE   Flags: Precursor;
GN   OrderedLocusNames=YPA_0526 {ECO:0000313|EMBL:ABG12494.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12494.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12494.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12494.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-
CC         1,2-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         Evidence={ECO:0000256|RuleBase:RU003938};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC       {ECO:0000256|RuleBase:RU003938}.
CC   -!- SIMILARITY: Belongs to the CDS family.
CC       {ECO:0000256|RuleBase:RU003938}.
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DR   EMBL; CP000308; ABG12494.1; -; Genomic_DNA.
DR   RefSeq; WP_002212137.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12494; ABG12494; YPA_0526.
DR   EnsemblBacteria; AJJ80641; AJJ80641; CH58_3378.
DR   KEGG; ypa:YPA_0526; -.
DR   PATRIC; fig|360102.15.peg.3547; -.
DR   KO; K00981; -.
DR   OMA; WEWGRLN; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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;
DR   PRODOM; A0A0E1NUT1.
DR   SWISS-2DPAGE; A0A0E1NUT1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Membrane {ECO:0000256|RuleBase:RU003938};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003938,
KW   ECO:0000313|EMBL:ABG12494.1};
KW   Transferase {ECO:0000256|RuleBase:RU003938,
KW   ECO:0000313|EMBL:ABG12494.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003938}.
SQ   SEQUENCE   282 AA;  31208 MW;  3679C2F0DC997070 CRC64;
     MLKYRLITAL ILIPVVIGAL FLLPPVGFAI VTLVVCMLAA WEWGQLAGFA SRTQRIWLAI
     LCGFLLVAML LSLPEYQHSP HHLLVSTPLW LSMGWWVAAL MLVLTYPRSA VSWRNSRLLR
     IIFGILTIIP FFWGMFALRQ YGYEQNHNTG AWWLLYVMLL VWGADSGAYM FGKLFGKHKL
     APKVSPGKTW EGLIGGLLTS ALISLLFGRY APLDIVPEKL LICSVVAALA SVLGDLTESM
     FKREAGIKDS GHLIPGHGGI LDRIDSLTAA VPVFACLMLL VF
//

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