DCTD_BPT4
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 03-AUG-2022, entry version 122.
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 Caudovirales; Myoviridae; 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 + 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;
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}.
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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 PDBsum; 1VQ2; -.
DR SMR; P16006; -.
DR DrugBank; DB04280; 3,4-Dihydro-2'-deoxyuridine-5'-monophosphate.
DR GeneID; 1258669; -.
DR KEGG; vg:1258669; -.
DR EvolutionaryTrace; P16006; -.
DR Proteomes; UP000009087; Genome.
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 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; PTHR11086; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
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 133..141
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
