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Protein

Deoxycytidylate deaminase

Gene

CD

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Supplies the nucleotide substrate for thymidylate synthetase.

Catalytic activityi

dCMP + H2O = dUMP + NH3.

Cofactori

Zn2+Note: Binds 2 Zn2+ 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
  2. pyrimidine nucleotide metabolic process Source: InterPro
Complete GO annotation...

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 Componenti: 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 – 1412Combined sources
Beta strandi20 – 223Combined sources
Beta strandi25 – 306Combined sources
Beta strandi33 – 397Combined sources
Helixi49 – 568Combined sources
Beta strandi59 – 613Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 903Combined sources
Helixi91 – 10111Combined sources
Helixi105 – 11612Combined sources
Beta strandi124 – 1296Combined sources
Helixi133 – 1419Combined sources
Beta strandi146 – 1516Combined sources
Turni158 – 1614Combined sources
Helixi162 – 1665Combined sources
Beta strandi170 – 1734Combined sources
Helixi176 – 1783Combined sources
Helixi184 – 1863Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP16006.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 171171CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK01493.

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. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCC
60 70 80 90 100
DYAAEQGWLL NKPKHAIIQG HKPECVSFGS TDRFVLAKEH RSAHSEWSSK
110 120 130 140 150
NEIHAELNAI LFAARNGSSI EGATMYVTLS PCPDCAKAIA QSGIKKLVYC
160 170 180 190
ETYDKNKPGW DDILRNAGIE VFNVPKKNLN KLNWENINEF CGE
Length:193
Mass (Da):21,198
Last modified:April 1, 1990 - v1
Checksum:iF720EF1B4A2E8CE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KEGGivg:1258669.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05172 Genomic DNA. Translation: AAA32489.1.
AF158101 Genomic DNA. Translation: AAD42546.1.
PIRiJN0081. DUBPT4.
RefSeqiNP_049828.1. NC_000866.4.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258669.
KEGGivg:1258669.

Phylogenomic databases

KOiK01493.

Miscellaneous databases

EvolutionaryTraceiP16006.

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. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1989) [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(1992) [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(2003) [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: April 1, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.