Reviewed, UniProtKB/Swiss-Prot P00814 (DCTD_BPT2)

Names and origin

Protein names

Recommended name:
    Deoxycytidylate deaminase
    EC=3.5.4.12
Alternative name(s):
    dCMP deaminase

Gene names

Name:

CD

Organism

Enterobacteria phage T2 (Bacteriophage T2)

Taxonomic identifier

10664 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › T4-like viruses

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
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	Allosteric enzyme Direct protein sequencing
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: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 188	188	Deoxycytidylate deaminase		PRO_0000171700
Sites
	Active site	106	1	Proton donor By similarity
	Metal binding	19	1	Zinc 1; structural By similarity
	Metal binding	49	1	Zinc 1; structural By similarity
	Metal binding	94	1	Zinc 1; structural By similarity
	Metal binding	102	1	Zinc 2; catalytic By similarity
	Metal binding	104	1	Zinc 2; catalytic By similarity
	Metal binding	132	1	Zinc 2; catalytic By similarity
	Metal binding	135	1	Zinc 2; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00814-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: A13EAF89D5CEB14A	FASTA	188	20,599
	10 20 30 40 50 60 MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCD NYAAIEGWLL 70 80 90 100 110 120 NKPKHTIIQG HKPECVSFGT SDRFVLAKEH RSAHSEWSSK NEIHAELNAI LFAARNGSSI 130 140 150 160 170 180 EGATMYVTLS PCPDCAKAIA QSGIKKLVYC ETYDKNKPGW DDILRNAGIE VFNVPKLNWE NISEFCGE

References

[1]	"Complete amino acid sequence of an allosteric enzyme, T2 bacteriophage deoxycytidylate deaminase." Maley G.F., Guarino D.U., Maley F. J. Biol. Chem. 258:8290-8297(1983) [PubMed: 6345541] [Abstract] Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases
PIR	DUBPC2. A01011.
3D structure databases
SMR	P00814. Positions 1-188.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.4.12. 142282.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR002125. CMP_dCMP_Zn_bd. IPR015517. Cyt_deaminase. IPR016473. dCMP_deaminase. [Graphical view]
PANTHER	PTHR11086. Cyt_deaminase. 1 hit.
Pfam	PF00383. dCMP_cyt_deam_1. 1 hit. [Graphical view]
PIRSF	PIRSF006019. dCMP_deaminase. 1 hit.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCTD_BPT2

Accession

Primary (citable) accession number: P00814

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)