DCTD_YEAST
ID DCTD_YEAST Reviewed; 312 AA.
AC P06773; D3DL94;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Deoxycytidylate deaminase {ECO:0000305};
DE EC=3.5.4.12 {ECO:0000305|PubMed:3023902};
DE AltName: Full=dCMP deaminase {ECO:0000303|PubMed:3023902};
GN Name=DCD1 {ECO:0000303|PubMed:3023902}; OrderedLocusNames=YHR144C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3023902; DOI=10.1128/mcb.6.5.1711-1721.1986;
RA McIntosh E.M., Haynes R.H.;
RT "Sequence and expression of the dCMP deaminase gene (DCD1) of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 6:1711-1721(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of dCMP to yield dUMP,
CC the nucleotide substrate for thymidylate synthetase.
CC {ECO:0000305|PubMed:3023902}.
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 Evidence={ECO:0000305|PubMed:3023902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22925;
CC Evidence={ECO:0000305|PubMed:3023902};
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 -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; M13010; AAA34561.1; -; Genomic_DNA.
DR EMBL; U10397; AAB68985.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06838.1; -; Genomic_DNA.
DR PIR; S46762; S46762.
DR RefSeq; NP_012014.1; NM_001179275.1.
DR AlphaFoldDB; P06773; -.
DR SMR; P06773; -.
DR BioGRID; 36578; 198.
DR DIP; DIP-4028N; -.
DR IntAct; P06773; 1.
DR MINT; P06773; -.
DR STRING; 4932.YHR144C; -.
DR MaxQB; P06773; -.
DR PaxDb; P06773; -.
DR PRIDE; P06773; -.
DR EnsemblFungi; YHR144C_mRNA; YHR144C; YHR144C.
DR GeneID; 856548; -.
DR KEGG; sce:YHR144C; -.
DR SGD; S000001187; DCD1.
DR VEuPathDB; FungiDB:YHR144C; -.
DR eggNOG; KOG3127; Eukaryota.
DR GeneTree; ENSGT00940000153676; -.
DR HOGENOM; CLU_047993_0_0_1; -.
DR InParanoid; P06773; -.
DR OMA; PPLRPDW; -.
DR BioCyc; MetaCyc:YHR144C-MON; -.
DR BioCyc; YEAST:YHR144C-MON; -.
DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:P06773; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P06773; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004132; F:dCMP deaminase activity; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006231; P:dTMP biosynthetic process; IMP:SGD.
DR GO; GO:0006226; P:dUMP biosynthetic process; IMP:SGD.
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; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR PANTHER; PTHR11086; PTHR11086; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 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 Allosteric enzyme; Hydrolase; Metal-binding; Nucleotide biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..312
FT /note="Deoxycytidylate deaminase"
FT /id="PRO_0000171697"
FT DOMAIN 162..291
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 78
FT /note="V -> A (in Ref. 1; AAA34561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35646 MW; 780B47CDA561D24B CRC64;
MLIGVSGTKF CGCEDVINML VDHFHFELLN HLDNPEEILD YATKNYTKNS VIFLEKLSLL
EKLEKRPFFV HLSIDAPVTT RVALYRKTTQ AESLSLEQII QAIDQHDFQP EGIKLREKSH
LRFKIVNEDR RGRRQSLINN ITTQLKILDD KEKQMAPLMR PSWDSYFMKL ATLAASRSNC
MKRRVGCVIV RECRVIATGY NGTPRHLTNC FNGGCPRCND GDSRNLHTCL CLHAEENALL
EAGRDRVGQN ATLYCDTCPC LTCSVKIVQT GISEVVYSQS YRMDEESFKV LKNAGITVRQ
FSFTEEPRIV MI
