ID   DCTD_BPT2               Reviewed;         188 AA.
AC   P00814;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Deoxycytidylate deaminase;
DE            EC=3.5.4.12;
DE   AltName: Full=dCMP deaminase;
GN   Name=CD;
OS   Enterobacteria phage T2 (Bacteriophage T2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Straboviridae; Tevenvirinae; Tequatrovirus; Tequatrovirus T2.
OX   NCBI_TaxID=2060721;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6345541; DOI=10.1016/s0021-9258(20)82063-8;
RA   Maley G.F., Guarino D.U., Maley F.;
RT   "Complete amino acid sequence of an allosteric enzyme, T2 bacteriophage
RT   deoxycytidylate deaminase.";
RL   J. Biol. Chem. 258:8290-8297(1983).
CC   -!- FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCMP + H(+) + H2O = dUMP + NH4(+); Xref=Rhea:RHEA:22924,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57566, ChEBI:CHEBI:246422; EC=3.5.4.12;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Allosteric enzyme whose activity is greatly
CC       influenced by the end products of its metabolic pathway, dCTP and dTTP.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   PIR; A01011; DUBPC2.
DR   SMR; P00814; -.
DR   GO; GO:0004132; F:dCMP deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:InterPro.
DR   CDD; cd01286; deoxycytidylate_deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR016473; dCMP_deaminase.
DR   InterPro; IPR015517; dCMP_deaminase-rel.
DR   InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR   PANTHER; PTHR11086:SF18; CYTIDINE AND DCMP DEAMINASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR11086; DEOXYCYTIDYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Nucleotide biosynthesis; Zinc.
FT   CHAIN           1..188
FT                   /note="Deoxycytidylate deaminase"
FT                   /id="PRO_0000171700"
FT   DOMAIN          1..171
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   188 AA;  20599 MW;  A13EAF89D5CEB14A CRC64;
     MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCD NYAAIEGWLL
     NKPKHTIIQG HKPECVSFGT SDRFVLAKEH RSAHSEWSSK NEIHAELNAI LFAARNGSSI
     EGATMYVTLS PCPDCAKAIA QSGIKKLVYC ETYDKNKPGW DDILRNAGIE VFNVPKLNWE
     NISEFCGE
//