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B0TQV3

- CDD_SHEHH

UniProt

B0TQV3 - CDD_SHEHH

Protein

Cytidine deaminase

Gene

cdd

Organism
Shewanella halifaxensis (strain HAW-EB4)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      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 bindingi101 – 1011Zinc; catalyticUniRule annotation
    Active sitei103 – 1031Proton donorUniRule annotation
    Metal bindingi128 – 1281Zinc; catalyticUniRule annotation
    Metal bindingi131 – 1311Zinc; 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

    BioCyciSHAL458817:GH1X-1842-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:Shal_1783
    OrganismiShewanella halifaxensis (strain HAW-EB4)
    Taxonomic identifieri458817 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
    ProteomesiUP000001317: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296Cytidine deaminasePRO_1000087798Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi458817.Shal_1783.

    Structurei

    3D structure databases

    ProteinModelPortaliB0TQV3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 13889CMP/dCMP deaminase zinc-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni88 – 903Substrate 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.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B0TQV3-1 [UniParc]FASTAAdd to Basket

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    MQDRFLKSIA KLPEPLATAI VPLLDKDFAG HIDAQQLEVL QIASKMELNE    50
    LLLALLPIAA ALARPPISEF HVGAIAKGKS GDIYMGANIE LPGEALFHSV 100
    HAEQSAISHA WLSGESIIED IIVNASPCGH CRQFINELVD GSKVKIHLPA 150
    QKIEPLAHYL PYAFGPSDLN ITEPLLTKQQ HTLTLDSNDP MIIEALDHAG 200
    LSYAPYTKNY ASVVLETKDG ATYCGRYAEN AAFNPSMQPM QMALSTMARH 250
    NRDFSEINRA VLIESSKGVI SLVGAAMDAL HSVAVVELEH IVVEPE 296
    Length:296
    Mass (Da):32,144
    Last modified:April 8, 2008 - v1
    Checksum:iBB0514870EB1ACBC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000931 Genomic DNA. Translation: ABZ76348.1.
    RefSeqiYP_001674007.1. NC_010334.1.

    Genome annotation databases

    EnsemblBacteriaiABZ76348; ABZ76348; Shal_1783.
    GeneIDi5903050.
    KEGGishl:Shal_1783.
    PATRICi23506241. VBISheHal24697_1871.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000931 Genomic DNA. Translation: ABZ76348.1 .
    RefSeqi YP_001674007.1. NC_010334.1.

    3D structure databases

    ProteinModelPortali B0TQV3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 458817.Shal_1783.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABZ76348 ; ABZ76348 ; Shal_1783 .
    GeneIDi 5903050.
    KEGGi shl:Shal_1783.
    PATRICi 23506241. VBISheHal24697_1871.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SHAL458817:GH1X-1842-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.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HAW-EB4.

    Entry informationi

    Entry nameiCDD_SHEHH
    AccessioniPrimary (citable) accession number: B0TQV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 40 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