ID DCTD_BPT4 Reviewed; 193 AA. AC P16006; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 10-JUN-2026, entry version 132. DE RecName: Full=Deoxycytidylate deaminase; DE EC=3.5.4.12; DE AltName: Full=dCMP deaminase; DE Short=dCD; GN Name=CD; OS Enterobacteria phage T4 (Bacteriophage T4). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Pantevenvirales; Straboviridae; Tevenvirinae; Tequatrovirus. OX NCBI_TaxID=10665; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2136740; DOI=10.1016/s0021-9258(19)40192-0; RA Maley G.F., Duceman B.W., Wang A.-M., Martinez J., Maley F.; RT "Cloning, sequence analysis, and expression of the bacteriophage T4 cd RT gene."; RL J. Biol. Chem. 265:47-51(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003; RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.; RT "Bacteriophage T4 genome."; RL Microbiol. Mol. Biol. Rev. 67:86-156(2003). RN [3] RP ZINC-BINDING. RX PubMed=8428902; DOI=10.1016/s0021-9258(18)53770-4; RA Moore J.T., Silversmith R.E., Maley G.F., Maley F.; RT "T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc RT atoms per subunit."; RL J. Biol. Chem. 268:2288-2291(1993). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLU-115 IN COMPLEX WITH RP SUBSTRATE ANALOG AND ZINC IONS. RX PubMed=15504034; DOI=10.1021/bi048928h; RA Almog R., Maley F., Maley G.F., Maccoll R., Van Roey P.; RT "Three-dimensional structure of the R115E mutant of T4-bacteriophage 2'- RT deoxycytidylate deaminase."; RL Biochemistry 43:13715-13723(2004). CC -!- FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase. CC -!- CATALYTIC ACTIVITY: CC Reaction=dCMP + H2O + H(+) = 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; CC Note=Binds 2 Zn(2+) ions per subunit.; 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. {ECO:0000269|PubMed:15504034}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05172; AAA32489.1; -; Genomic_DNA. DR EMBL; AF158101; AAD42546.1; -; Genomic_DNA. DR PIR; JN0081; DUBPT4. DR RefSeq; NP_049828.1; NC_000866.4. DR PDB; 1VQ2; X-ray; 2.20 A; A=1-193. DR SMR; P16006; -. DR DrugBank; DB04280; 3,4-Dihydro-2'-deoxyuridine-5'-monophosphate. DR GeneID; 1258669; -. DR KEGG; vg:1258669; -. DR OrthoDB; 10605at10239; -. DR EvolutionaryTrace; P16006; -. DR Proteomes; UP000009087; Segment. 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 DisProt; DP00583; -. 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; DEOXYCYTIDYLATE DEAMINASE; 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. DR PDBsum; 1VQ2; -. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Hydrolase; Metal-binding; KW Nucleotide biosynthesis; Reference proteome; Zinc. FT CHAIN 1..193 FT /note="Deoxycytidylate deaminase" FT /id="PRO_0000171699" 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 BINDING 49 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT BINDING 94 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT BINDING 153 FT /ligand="substrate" FT HELIX 3..14 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 20..22 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 25..30 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 49..56 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 91..101 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 105..116 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 133..142 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:1VQ2" FT TURN 158..161 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 162..166 FT /evidence="ECO:0007829|PDB:1VQ2" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:1VQ2" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:1VQ2" SQ SEQUENCE 193 AA; 21198 MW; F720EF1B4A2E8CE6 CRC64; MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCC DYAAEQGWLL NKPKHAIIQG HKPECVSFGS TDRFVLAKEH RSAHSEWSSK NEIHAELNAI LFAARNGSSI EGATMYVTLS PCPDCAKAIA QSGIKKLVYC ETYDKNKPGW DDILRNAGIE VFNVPKKNLN KLNWENINEF CGE //