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P0ABG3

- CDSA_SHIFL

UniProt

P0ABG3 - CDSA_SHIFL

Protein

Phosphatidate cytidylyltransferase

Gene

cdsA

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

    Pathwayi

    GO - Molecular functioni

    1. phosphatidate cytidylyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Enzyme and pathway databases

    UniPathwayiUPA00557; UER00614.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidate cytidylyltransferase (EC:2.7.7.41)
    Alternative name(s):
    CDP-DAG synthase
    CDP-DG synthase
    CDP-diacylglycerol synthase
    Short name:
    CDS
    CDP-diglyceride pyrophosphorylase
    CDP-diglyceride synthase
    CTP:phosphatidate cytidylyltransferase
    Gene namesi
    Name:cdsA
    Ordered Locus Names:SF0165, S0168
    OrganismiShigella flexneri
    Taxonomic identifieri623 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 285285Phosphatidate cytidylyltransferasePRO_0000090746Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi198214.SF0165.

    Structurei

    3D structure databases

    ProteinModelPortaliP0ABG3.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 3021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei56 – 7621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei93 – 11321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei121 – 14121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei151 – 17121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei190 – 21021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei213 – 23321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei264 – 28421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CDS family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0575.
    HOGENOMiHOG000006168.
    KOiK00981.
    OMAiYVFILVW.
    OrthoDBiEOG6TBHJT.

    Family and domain databases

    InterProiIPR000374. PC_trans.
    [Graphical view]
    PfamiPF01148. CTP_transf_1. 1 hit.
    [Graphical view]
    PROSITEiPS01315. CDS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ABG3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKYRLISAF VLIPVVIAAL FLLPPVGFAI VTLVVCMLAA WEWGQLSGFT    50
    TRSQRVWLAV LCGLLLALML FLLPEYHRNI HQPLVEISLW ASLGWWIVAL 100
    LLVLFYPGSA AIWRNSKTLR LIFGVLTIVP FFWGMLALRA WHYDENHYSG 150
    AIWLLYVMIL VWGADSGAYM FGKLFGKHKL APKVSPGKTW QGFIGGLATA 200
    AVISWGYGMW ANLDVAPVTL LICSIVAALA SVLGDLTESM FKREAGIKDS 250
    GHLIPGHGGI LDRIDSLTAA VPVFACLLLL VFRTL 285
    Length:285
    Mass (Da):31,454
    Last modified:November 13, 2007 - v2
    Checksum:i0D77DCD5EC5FBA9F
    GO

    Sequence cautioni

    The sequence AAN41827.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAP15708.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN41827.2. Different initiation.
    AE014073 Genomic DNA. Translation: AAP15708.1. Different initiation.
    RefSeqiNP_706120.4. NC_004337.2.
    NP_835903.2. NC_004741.1.

    Genome annotation databases

    EnsemblBacteriaiAAN41827; AAN41827; SF0165.
    AAP15708; AAP15708; S0168.
    GeneIDi1024478.
    1076599.
    KEGGisfl:SF0165.
    sfx:S0168.
    PATRICi18701288. VBIShiFle31049_0185.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN41827.2 . Different initiation.
    AE014073 Genomic DNA. Translation: AAP15708.1 . Different initiation.
    RefSeqi NP_706120.4. NC_004337.2.
    NP_835903.2. NC_004741.1.

    3D structure databases

    ProteinModelPortali P0ABG3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198214.SF0165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN41827 ; AAN41827 ; SF0165 .
    AAP15708 ; AAP15708 ; S0168 .
    GeneIDi 1024478.
    1076599.
    KEGGi sfl:SF0165.
    sfx:S0168.
    PATRICi 18701288. VBIShiFle31049_0185.

    Phylogenomic databases

    eggNOGi COG0575.
    HOGENOMi HOG000006168.
    KOi K00981.
    OMAi YVFILVW.
    OrthoDBi EOG6TBHJT.

    Enzyme and pathway databases

    UniPathwayi UPA00557 ; UER00614 .

    Family and domain databases

    InterProi IPR000374. PC_trans.
    [Graphical view ]
    Pfami PF01148. CTP_transf_1. 1 hit.
    [Graphical view ]
    PROSITEi PS01315. CDS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
      Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
      , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
      Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 301 / Serotype 2a.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700930 / 2457T / Serotype 2a.

    Entry informationi

    Entry nameiCDSA_SHIFL
    AccessioniPrimary (citable) accession number: P0ABG3
    Secondary accession number(s): P06466
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 69 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3