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P16006 (DCTD_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxycytidylate deaminase

EC=3.5.4.12
Alternative name(s):
dCMP deaminase
Short name=dCD
Gene names
Name:CD
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Supplies the nucleotide substrate for thymidylate synthetase.

Catalytic activity

dCMP + H2O = dUMP + NH3.

Cofactor

Binds 2 zinc ions per subunit.

Enzyme regulation

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

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondCMP deaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Deoxycytidylate deaminase
PRO_0000171699

Sites

Active site1061Proton donor By similarity
Metal binding191Zinc 1; structural
Metal binding491Zinc 1; structural
Metal binding941Zinc 1; structural
Metal binding1021Zinc 2; structural
Metal binding1041Zinc 2; catalytic
Metal binding1321Zinc 2; catalytic
Metal binding1351Zinc 2; catalytic
Binding site1531Substrate

Secondary structure

................................... 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16006 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: F720EF1B4A2E8CE6

FASTA19321,198
        10         20         30         40         50         60 
MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCC DYAAEQGWLL 

        70         80         90        100        110        120 
NKPKHAIIQG HKPECVSFGS TDRFVLAKEH RSAHSEWSSK NEIHAELNAI LFAARNGSSI 

       130        140        150        160        170        180 
EGATMYVTLS PCPDCAKAIA QSGIKKLVYC ETYDKNKPGW DDILRNAGIE VFNVPKKNLN 

       190 
KLNWENINEF CGE 

« Hide

References

« Hide 'large scale' references
[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]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05172 Genomic DNA. Translation: AAA32489.1.
AF158101 Genomic DNA. Translation: AAD42546.1.
PIRDUBPT4. JN0081.
RefSeqNP_049828.1. NC_000866.4.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VQ2X-ray2.20A1-193[»]
DisProtDP00583.
ProteinModelPortalP16006.
SMRP16006. Positions 1-193.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258669.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR015517. Cyt_deaminase.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
[Graphical view]
PANTHERPTHR11086. PTHR11086. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMSSF53927. SSF53927. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16006.

Entry information

Entry nameDCTD_BPT4
AccessionPrimary (citable) accession number: P16006
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 14, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references