DCTD_BPMD2
ID DCTD_BPMD2 Reviewed; 128 AA.
AC O22000;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Deoxycytidylate deaminase;
DE EC=3.5.4.12;
DE AltName: Full=dCMP deaminase;
GN Name=36.1; Synonyms=G1;
OS Mycobacterium phage D29 (Mycobacteriophage D29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Fromanvirus.
OX NCBI_TaxID=28369;
OH NCBI_TaxID=1763; Mycobacterium.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9636706; DOI=10.1006/jmbi.1997.1610;
RA Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.;
RT "Genome structure of mycobacteriophage D29: implications for phage
RT evolution.";
RL J. Mol. Biol. 279:143-164(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-128.
RX PubMed=9274023; DOI=10.1099/00221287-143-8-2701;
RA Ribeiro G., Viveiros M., David H.L., Costa J.V.;
RT "Mycobacteriophage D29 contains an integration system similar to that of
RT the temperate mycobacteriophage L5.";
RL Microbiology 143:2701-2708(1997).
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 -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AF022214; AAC18478.1; -; Genomic_DNA.
DR EMBL; U81553; AAB69099.1; -; Genomic_DNA.
DR PIR; C72804; C72804.
DR RefSeq; NP_046853.1; NC_001900.1.
DR SMR; O22000; -.
DR GeneID; 1261565; -.
DR KEGG; vg:1261565; -.
DR Proteomes; UP000002131; 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 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 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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..128
FT /note="Deoxycytidylate deaminase"
FT /id="PRO_0000171698"
FT DOMAIN 5..128
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 128 AA; 13539 MW; F78F1BA3DB5184D4 CRC64;
MSRPDWDEYF LGIATAAAQR SDCERSKVGA VVVKDRRVRG TGYNGAPAGA AGCSTCPRRL
SGAVPGVSDY SSGATRCVAV HAEANALLYC DREDLIGATL YVTREPCYAC SNLIAASGIE
RVVYPKES
