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A8A204

- CDD_ECOHS

UniProt

A8A204 - CDD_ECOHS

Protein

Cytidine deaminase

Gene

cdd

Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      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

    BioCyciECOL331112:GHHI-2264-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:EcHS_A2277
    OrganismiEscherichia coli O9:H4 (strain HS)
    Taxonomic identifieri331112 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001123: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 294294Cytidine deaminasePRO_1000068949Add
    BLAST

    Proteomic databases

    PRIDEiA8A204.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi331112.EcHS_A2277.

    Structurei

    3D structure databases

    ProteinModelPortaliA8A204.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 13984CMP/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.

    A8A204-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED    50
    ALAFALLPLA AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT 100
    VHAEQSAISH AWLSGEKALA AITVNYTPCG HCRQFMNELN SGLDLRIHLP 150
    GREAHALRDY LPDAFGPKDL EIKTLLMDEQ DHGYALTGDA LSQAAIAAAN 200
    RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL QGALILLNLK 250
    GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHSIDR VLLA 294
    Length:294
    Mass (Da):31,540
    Last modified:October 23, 2007 - v1
    Checksum:iF0B5CD68AB145D7D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000802 Genomic DNA. Translation: ABV06558.1.
    RefSeqiYP_001458941.1. NC_009800.1.

    Genome annotation databases

    EnsemblBacteriaiABV06558; ABV06558; EcHS_A2277.
    GeneIDi5592274.
    KEGGiecx:EcHS_A2277.
    PATRICi18314536. VBIEscCol77814_2231.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000802 Genomic DNA. Translation: ABV06558.1 .
    RefSeqi YP_001458941.1. NC_009800.1.

    3D structure databases

    ProteinModelPortali A8A204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 331112.EcHS_A2277.

    Proteomic databases

    PRIDEi A8A204.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV06558 ; ABV06558 ; EcHS_A2277 .
    GeneIDi 5592274.
    KEGGi ecx:EcHS_A2277.
    PATRICi 18314536. VBIEscCol77814_2231.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ECOL331112:GHHI-2264-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. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
      Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
      J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HS.

    Entry informationi

    Entry nameiCDD_ECOHS
    AccessioniPrimary (citable) accession number: A8A204
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 47 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