ID   DCTD_PONAB              Reviewed;         178 AA.
AC   Q5RC69;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Deoxycytidylate deaminase;
DE            EC=3.5.4.12;
DE   AltName: Full=dCMP deaminase;
GN   Name=DCTD;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.
CC       {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Allosteric enzyme whose activity is greatly
CC       influenced by the end products of its metabolic pathway, dCTP and dTTP.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; CR858411; CAH90638.1; -; mRNA.
DR   RefSeq; XP_009238756.1; XM_009240481.1.
DR   AlphaFoldDB; Q5RC69; -.
DR   SMR; Q5RC69; -.
DR   STRING; 9601.ENSPPYP00000017005; -.
DR   Ensembl; ENSPPYT00000017695; ENSPPYP00000017005; ENSPPYG00000015223.
DR   GeneID; 100457791; -.
DR   KEGG; pon:100457791; -.
DR   CTD; 1635; -.
DR   eggNOG; KOG3127; Eukaryota.
DR   GeneTree; ENSGT00940000153676; -.
DR   HOGENOM; CLU_047993_1_1_1; -.
DR   InParanoid; Q5RC69; -.
DR   OMA; LMFEMAG; -.
DR   OrthoDB; 1569973at2759; -.
DR   TreeFam; TF105971; -.
DR   Proteomes; UP000001595; Chromosome 4.
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   2: Evidence at transcript level;
KW   Allosteric enzyme; Hydrolase; Metal-binding; Nucleotide biosynthesis;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..178
FT                   /note="Deoxycytidylate deaminase"
FT                   /id="PRO_0000171693"
FT   DOMAIN          14..146
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        86
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
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"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32321"
SQ   SEQUENCE   178 AA;  20045 MW;  7829EA3F433280BD CRC64;
     MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG IGYNGMPNGC
     SDDQLPWRRT AKNKLDTKYP YVCHAELNAI MNKNSTDVKG CSMYVALFPC NECAKLIIQA
     GIKEVIFMSD KYHDSDEATA ARLLFDMAGV TFRKFIPKCS KIVIDFDSIN SRPSQKLQ