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C6DDS7

- CDD_PECCP

UniProt

C6DDS7 - CDD_PECCP

Protein

Cytidine deaminase

Gene

cdd

Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 34 (01 Oct 2014)
      Sequence version 1 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.UniRule annotation

    Catalytic activityi

    Cytidine + H2O = uridine + NH3.UniRule annotation
    2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.UniRule annotation

    Cofactori

    Binds 1 zinc ion.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi102 – 1021Zinc; catalyticUniRule annotation
    Active sitei104 – 1041Proton donorUniRule annotation
    Metal bindingi129 – 1291Zinc; catalyticUniRule annotation
    Metal bindingi132 – 1321Zinc; catalyticUniRule annotation

    GO - Molecular functioni

    1. cytidine deaminase activity Source: UniProtKB-HAMAP
    2. zinc ion binding Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciPCAR561230:GKCK-1537-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytidine deaminaseUniRule annotation (EC:3.5.4.5UniRule annotation)
    Alternative name(s):
    Cytidine aminohydrolaseUniRule annotation
    Short name:
    CDAUniRule annotation
    Gene namesi
    Name:cddUniRule annotation
    Ordered Locus Names:PC1_1495
    OrganismiPectobacterium carotovorum subsp. carotovorum (strain PC1)
    Taxonomic identifieri561230 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
    ProteomesiUP000002736: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296Cytidine deaminasePRO_1000215505Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi561230.PC1_1495.

    Structurei

    3D structure databases

    ProteinModelPortaliC6DDS7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 14084CMP/dCMP deaminase zinc-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni89 – 913Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the cytidine and deoxycytidylate deaminase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0295.
    HOGENOMiHOG000218617.
    KOiK01489.
    OMAiNRSHAPY.
    OrthoDBiEOG6XDH25.

    Family and domain databases

    HAMAPiMF_01558. Cyt_deam.
    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR013171. Cyd/dCyd_deaminase_Zn-bd.
    IPR006263. Cyt_deam_dimer.
    IPR016193. Cytidine_deaminase-like.
    IPR020797. Cytidine_deaminase_bacteria.
    [Graphical view]
    PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
    PF08211. dCMP_cyt_deam_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006334. Cdd_plus_pseudo. 1 hit.
    SUPFAMiSSF53927. SSF53927. 2 hits.
    TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C6DDS7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHPRFENAFR QLPASLQAAL RPLIDKPDFA AMLTADDVNA VCEASQLDAD    50
    ALAFALLPLA AACAQAPISN FQVGAIAQGL SGNFYFGANM EFSAVQLQQT 100
    VHAEQSAVSH AWMRNERGLR AVTVNYTPCG HCRQFMNELR DAASLRIQLP 150
    GRQPATLSHY LPDSFGPVDL QIDTLLMDDI NHGATLQNMN ALARQALDAA 200
    NRSHAPYSKA ISGIVLETSS GNTYTGRYAE NAAFNPSLPP LQTALNLMNL 250
    AGEDLSTVKH AVVVERRNAV VSHWAISQIM LAELGCTDVE HHFIEE 296
    Length:296
    Mass (Da):32,120
    Last modified:September 1, 2009 - v1
    Checksum:i44DDC91C25AA3485
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001657 Genomic DNA. Translation: ACT12539.1.
    RefSeqiWP_015839765.1. NC_012917.1.
    YP_003017075.1. NC_012917.1.

    Genome annotation databases

    EnsemblBacteriaiACT12539; ACT12539; PC1_1495.
    GeneIDi8132436.
    KEGGipct:PC1_1495.
    PATRICi20487638. VBIPecCar70489_1508.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001657 Genomic DNA. Translation: ACT12539.1 .
    RefSeqi WP_015839765.1. NC_012917.1.
    YP_003017075.1. NC_012917.1.

    3D structure databases

    ProteinModelPortali C6DDS7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 561230.PC1_1495.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACT12539 ; ACT12539 ; PC1_1495 .
    GeneIDi 8132436.
    KEGGi pct:PC1_1495.
    PATRICi 20487638. VBIPecCar70489_1508.

    Phylogenomic databases

    eggNOGi COG0295.
    HOGENOMi HOG000218617.
    KOi K01489.
    OMAi NRSHAPY.
    OrthoDBi EOG6XDH25.

    Enzyme and pathway databases

    BioCyci PCAR561230:GKCK-1537-MONOMER.

    Family and domain databases

    HAMAPi MF_01558. Cyt_deam.
    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR013171. Cyd/dCyd_deaminase_Zn-bd.
    IPR006263. Cyt_deam_dimer.
    IPR016193. Cytidine_deaminase-like.
    IPR020797. Cytidine_deaminase_bacteria.
    [Graphical view ]
    Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
    PF08211. dCMP_cyt_deam_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006334. Cdd_plus_pseudo. 1 hit.
    SUPFAMi SSF53927. SSF53927. 2 hits.
    TIGRFAMsi TIGR01355. cyt_deam_dimer. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.
      , Balakrishnan V., Glasner J., Perna N.T.
      Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PC1.

    Entry informationi

    Entry nameiCDD_PECCP
    AccessioniPrimary (citable) accession number: C6DDS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 34 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3