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P16006

- DCTD_BPT4

UniProt

P16006 - DCTD_BPT4

Protein

Deoxycytidylate deaminase

Gene

CD

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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.

    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; structural
    Metal bindingi49 – 491Zinc 1; structural
    Metal bindingi94 – 941Zinc 1; structural
    Metal bindingi102 – 1021Zinc 2; structural
    Metal bindingi104 – 1041Zinc 2; catalytic
    Active sitei106 – 1061Proton donorBy similarity
    Metal bindingi132 – 1321Zinc 2; catalytic
    Metal bindingi135 – 1351Zinc 2; catalytic
    Binding sitei153 – 1531Substrate

    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
    Short name:
    dCD
    Gene namesi
    Name:CD
    OrganismiEnterobacteria phage T4 (Bacteriophage T4)
    Taxonomic identifieri10665 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
    Virus hostiEscherichia coli [TaxID: 562]
    ProteomesiUP000009087: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 193193Deoxycytidylate deaminasePRO_0000171699Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1412
    Beta strandi20 – 223
    Beta strandi25 – 306
    Beta strandi33 – 397
    Helixi49 – 568
    Beta strandi59 – 613
    Beta strandi84 – 863
    Helixi88 – 903
    Helixi91 – 10111
    Helixi105 – 11612
    Beta strandi124 – 1296
    Helixi133 – 1419
    Beta strandi146 – 1516
    Turni158 – 1614
    Helixi162 – 1665
    Beta strandi170 – 1734
    Helixi176 – 1783
    Helixi184 – 1863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VQ2X-ray2.20A1-193[»]
    DisProtiDP00583.
    ProteinModelPortaliP16006.
    SMRiP16006. Positions 1-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16006.

    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.

    P16006-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCC    50
    DYAAEQGWLL NKPKHAIIQG HKPECVSFGS TDRFVLAKEH RSAHSEWSSK 100
    NEIHAELNAI LFAARNGSSI EGATMYVTLS PCPDCAKAIA QSGIKKLVYC 150
    ETYDKNKPGW DDILRNAGIE VFNVPKKNLN KLNWENINEF CGE 193
    Length:193
    Mass (Da):21,198
    Last modified:April 1, 1990 - v1
    Checksum:iF720EF1B4A2E8CE6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05172 Genomic DNA. Translation: AAA32489.1.
    AF158101 Genomic DNA. Translation: AAD42546.1.
    PIRiJN0081. DUBPT4.
    RefSeqiNP_049828.1. NC_000866.4.

    Genome annotation databases

    GeneIDi1258669.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05172 Genomic DNA. Translation: AAA32489.1 .
    AF158101 Genomic DNA. Translation: AAD42546.1 .
    PIRi JN0081. DUBPT4.
    RefSeqi NP_049828.1. NC_000866.4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VQ2 X-ray 2.20 A 1-193 [» ]
    DisProti DP00583.
    ProteinModelPortali P16006.
    SMRi P16006. Positions 1-193.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1258669.

    Miscellaneous databases

    EvolutionaryTracei P16006.

    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. "Cloning, sequence analysis, and expression of the bacteriophage T4 cd gene."
      Maley G.F., Duceman B.W., Wang A.-M., Martinez J., Maley F.
      J. Biol. Chem. 265:47-51(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit."
      Moore J.T., Silversmith R.E., Maley G.F., Maley F.
      J. Biol. Chem. 268:2288-2291(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC-BINDING.
    4. "Three-dimensional structure of the R115E mutant of T4-bacteriophage 2'-deoxycytidylate deaminase."
      Almog R., Maley F., Maley G.F., Maccoll R., Van Roey P.
      Biochemistry 43:13715-13723(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLU-115 IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS.

    Entry informationi

    Entry nameiDCTD_BPT4
    AccessioniPrimary (citable) accession number: P16006
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 96 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

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3