P16006 (DCTD_BPT4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxycytidylate deaminase
EC=3.5.4.12

Alternative name(s):
dCMP deaminase
Short name=dCD

Gene names

Name:

CD

Organism

Enterobacteria phage T4 (Bacteriophage T4) [Reference proteome]

Taxonomic identifier

10665 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus › Enterobacteria phage T4 sensu lato

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Nucleotide biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	dCMP deaminase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 193

193

Deoxycytidylate deaminase

PRO_0000171699

Sites

Active site

106

1

Proton donor By similarity

Metal binding

19

1

Zinc 1; structural

Metal binding

49

1

Zinc 1; structural

Metal binding

94

1

Zinc 1; structural

Metal binding

102

1

Zinc 2; structural

Metal binding

104

1

Zinc 2; catalytic

Metal binding

132

1

Zinc 2; catalytic

Metal binding

135

1

Zinc 2; catalytic

Binding site

153

1

Substrate

Secondary structure

1

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193

Helix Strand Turn

Details...

Helix

3 – 14

12

Beta strand

20 – 22

3

Beta strand

25 – 30

6

Beta strand

33 – 39

7

Helix

49 – 56

8

Beta strand

59 – 61

3

Beta strand

84 – 86

3

Helix

88 – 90

3

Helix

91 – 101

11

Helix

105 – 116

12

Beta strand

124 – 129

6

Helix

133 – 141

9

Beta strand

146 – 151

6

Turn

158 – 161

4

Helix

162 – 166

5

Beta strand

170 – 173

4

Helix

176 – 178

3

Helix

184 – 186

3

Sequences

	Sequence		Length	Mass (Da)
	P16006 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: F720EF1B4A2E8CE6	FASTA	193	21,198
	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

References

	« Hide 'large scale' referencesShow '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.

PIR

DUBPT4. JN0081.

RefSeq

NP_049828.1. NC_000866.4.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VQ2	X-ray	2.20	A	1-193	[»]

ProteinModelPortal

P16006.

SMR

P16006. Positions 1-193.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1258669.

Phylogenomic databases

ProtClustDB

PHA2588.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR015517. Cyt_deaminase.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
[Graphical view]

PANTHER

PTHR11086. PTHR11086. 1 hit.

Pfam

PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]

PIRSF

PIRSF006019. dCMP_deaminase. 1 hit.

SUPFAM

SSF53927. Cytidine_deaminase-like. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P16006.

Entry information

Entry name

DCTD_BPT4

Accession

Primary (citable) accession number: P16006

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program