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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)DescriptionActionsGraphical viewLength
Metal bindingi19Zinc 1; structural1
Metal bindingi49Zinc 1; structural1
Metal bindingi94Zinc 1; structural1
Metal bindingi102Zinc 2; structural1
Metal bindingi104Zinc 2; catalytic1
Active sitei106Proton donorBy similarity1
Metal bindingi132Zinc 2; catalytic1
Metal bindingi135Zinc 2; catalytic1
Binding sitei153Substrate1

GO - Molecular functioni

GO - Biological processi

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]
Proteomesi
  • UP000009087 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001716991 – 193Deoxycytidylate deaminaseAdd BLAST193

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 14Combined sources12
Beta strandi20 – 22Combined sources3
Beta strandi25 – 30Combined sources6
Beta strandi33 – 39Combined sources7
Helixi49 – 56Combined sources8
Beta strandi59 – 61Combined sources3
Beta strandi84 – 86Combined sources3
Helixi88 – 90Combined sources3
Helixi91 – 101Combined sources11
Helixi105 – 116Combined sources12
Beta strandi124 – 129Combined sources6
Helixi133 – 141Combined sources9
Beta strandi146 – 151Combined sources6
Turni158 – 161Combined sources4
Helixi162 – 166Combined sources5
Beta strandi170 – 173Combined sources4
Helixi176 – 178Combined sources3
Helixi184 – 186Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP16006.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 171CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST171

Sequence similaritiesi

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

Phylogenomic databases

KOiK01493.

Family and domain databases

CDDicd01286. deoxycytidylate_deaminase. 1 hit.
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. 2 hits.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VQ2X-ray2.20A1-193[»]
DisProtiDP00583.
ProteinModelPortaliP16006.
SMRiP16006.
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

CDDicd01286. deoxycytidylate_deaminase. 1 hit.
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. 2 hits.
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...

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: November 2, 2016
This is version 105 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

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 one 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.