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P00814

- DCTD_BPT2

UniProt

P00814 - DCTD_BPT2

Protein

Deoxycytidylate deaminase

Gene

CD

Organism
Enterobacteria phage T2 (Bacteriophage T2)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Supplies the nucleotide substrate for thymidylate synthetase.

    Catalytic activityi

    dCMP + H2O = dUMP + NH3.

    Cofactori

    Binds 2 zinc ions per subunit.By similarity

    Enzyme regulationi

    Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi19 – 191Zinc 1; structuralBy similarity
    Metal bindingi49 – 491Zinc 1; structuralBy similarity
    Metal bindingi94 – 941Zinc 1; structuralBy similarity
    Metal bindingi102 – 1021Zinc 2; catalyticBy similarity
    Metal bindingi104 – 1041Zinc 2; catalyticBy similarity
    Active sitei106 – 1061Proton donorBy similarity
    Metal bindingi132 – 1321Zinc 2; catalyticBy similarity
    Metal bindingi135 – 1351Zinc 2; catalyticBy similarity

    GO - Molecular functioni

    1. dCMP deaminase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. nucleotide biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxycytidylate deaminase (EC:3.5.4.12)
    Alternative name(s):
    dCMP deaminase
    Gene namesi
    Name:CD
    OrganismiEnterobacteria phage T2 (Bacteriophage T2)
    Taxonomic identifieri10664 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
    Virus hostiEscherichia coli [TaxID: 562]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188Deoxycytidylate deaminasePRO_0000171700Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.

    Structurei

    3D structure databases

    ProteinModelPortaliP00814.
    SMRiP00814. Positions 1-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR016193. Cytidine_deaminase-like.
    IPR016473. dCMP_deaminase.
    IPR015517. dCMP_deaminase-rel.
    [Graphical view]
    PANTHERiPTHR11086. PTHR11086. 1 hit.
    PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
    SUPFAMiSSF53927. SSF53927. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00814-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCD    50
    NYAAIEGWLL NKPKHTIIQG HKPECVSFGT SDRFVLAKEH RSAHSEWSSK 100
    NEIHAELNAI LFAARNGSSI EGATMYVTLS PCPDCAKAIA QSGIKKLVYC 150
    ETYDKNKPGW DDILRNAGIE VFNVPKLNWE NISEFCGE 188
    Length:188
    Mass (Da):20,599
    Last modified:July 21, 1986 - v1
    Checksum:iA13EAF89D5CEB14A
    GO

    Sequence databases

    PIRiA01011. DUBPC2.

    Cross-referencesi

    Sequence databases

    PIRi A01011. DUBPC2.

    3D structure databases

    ProteinModelPortali P00814.
    SMRi P00814. Positions 1-188.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR016193. Cytidine_deaminase-like.
    IPR016473. dCMP_deaminase.
    IPR015517. dCMP_deaminase-rel.
    [Graphical view ]
    PANTHERi PTHR11086. PTHR11086. 1 hit.
    Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006019. dCMP_deaminase. 1 hit.
    SUPFAMi SSF53927. SSF53927. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete amino acid sequence of an allosteric enzyme, T2 bacteriophage deoxycytidylate deaminase."
      Maley G.F., Guarino D.U., Maley F.
      J. Biol. Chem. 258:8290-8297(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiDCTD_BPT2
    AccessioniPrimary (citable) accession number: P00814
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3