Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q87Q52

- CDD_VIBPA

UniProt

Q87Q52 - CDD_VIBPA

Protein

Cytidine deaminase

Gene

cdd

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    BioCyciVPAR223926:GHK4-1347-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:VP1298
    OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
    Taxonomic identifieri223926 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000002493: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Cytidine deaminasePRO_0000171671Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi223926.VP1298.

    Structurei

    3D structure databases

    ProteinModelPortaliQ87Q52.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini60 – 14283CMP/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.

    Q87Q52-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSRIEQALA SAPEALSKQL APIVLADDFD ATLSAQQFEQ LLSATSLSDK    50
    ELRVALLPFA AAYSYAPISE FYVGAIVRGL SGRLYFGANM EFFGVQLGQT 100
    VHAEQSAISH AWMKGEHGVK DITINFSPCG HCRQFMNELS TAKELKVQLP 150
    ERDEKSLHEY LPEAFGPADL GIESGLMAEV KHQFVCDDKD ALIQQAVEAM 200
    NMSHAPYTNN LSGLALELAN GRVFKGAYAE NAAFNPSLPP LQVALIQVLL 250
    AGETFDSIKA AALVENSEGK ISHLADTQST LEALNPDIPV SFVNV 295
    Length:295
    Mass (Da):31,912
    Last modified:June 1, 2003 - v1
    Checksum:i215BA72CE1F958BF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC59561.1.
    RefSeqiNP_797677.1. NC_004603.1.

    Genome annotation databases

    EnsemblBacteriaiBAC59561; BAC59561; BAC59561.
    GeneIDi1188803.
    KEGGivpa:VP1298.
    PATRICi20140802. VBIVibPar50997_1238.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC59561.1 .
    RefSeqi NP_797677.1. NC_004603.1.

    3D structure databases

    ProteinModelPortali Q87Q52.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 223926.VP1298.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC59561 ; BAC59561 ; BAC59561 .
    GeneIDi 1188803.
    KEGGi vpa:VP1298.
    PATRICi 20140802. VBIVibPar50997_1238.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci VPAR223926:GHK4-1347-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. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
      Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
      Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RIMD 2210633.

    Entry informationi

    Entry nameiCDD_VIBPA
    AccessioniPrimary (citable) accession number: Q87Q52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 74 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3