DDI2_YEAST
ID DDI2_YEAST Reviewed; 225 AA.
AC P0CH63; D6VTG9; P43543;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cyanamide hydratase DDI2 {ECO:0000303|PubMed:25847245};
DE Short=CAH {ECO:0000303|PubMed:25847245};
DE EC=4.2.1.69 {ECO:0000269|PubMed:25847245};
DE AltName: Full=DNA damage-inducible protein 2 {ECO:0000303|PubMed:18485869};
GN Name=DDI2 {ECO:0000303|PubMed:18485869};
GN OrderedLocusNames=YFL061W {ECO:0000312|SGD:S000001833};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INDUCTION.
RX PubMed=18485869; DOI=10.1016/j.cell.2008.02.050;
RA Fu Y., Zhu Y., Zhang K., Yeung M., Durocher D., Xiao W.;
RT "Rad6-Rad18 mediates a eukaryotic SOS response by ubiquitinating the 9-1-1
RT checkpoint clamp.";
RL Cell 133:601-611(2008).
RN [5]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25847245; DOI=10.1074/jbc.m115.645408;
RA Li J., Biss M., Fu Y., Xu X., Moore S.A., Xiao W.;
RT "Two duplicated genes DDI2 and DDI3 in budding yeast encode a cyanamide
RT hydratase and are induced by cyanamide.";
RL J. Biol. Chem. 290:12664-12675(2015).
CC -!- FUNCTION: Cyanamide hydratase involved in the detoxification and/or
CC utilization of cyanamide, a toxic nitrile compound distributed widely
CC in the environment. {ECO:0000269|PubMed:25847245}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69;
CC Evidence={ECO:0000269|PubMed:25847245};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P22143};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.3 mM for cyanamide {ECO:0000269|PubMed:25847245};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P22143}.
CC -!- INDUCTION: Expression is induced by DNA-damaging agents such as methyl
CC methanesulfonate (MMS) or dimethyl sulfate (DMS) (PubMed:18485869,
CC PubMed:25847245). Massively induced by cyanamide (PubMed:25847245).
CC {ECO:0000269|PubMed:18485869, ECO:0000269|PubMed:25847245}.
CC -!- DISRUPTION PHENOTYPE: The double deletion of DDI2 and DDI3 compromizes
CC cellular resistance to cyanamide by impairing its metabolization.
CC {ECO:0000269|PubMed:25847245}.
CC -!- MISCELLANEOUS: DDI2 and DDI3 are duplicated genes located on different
CC chromosomes, with identical ORF sequences and only one nucleotide
CC difference in their promoter (up to 1 kb) regions.
CC {ECO:0000303|PubMed:25847245}.
CC -!- SIMILARITY: Belongs to the cyanamide dehydrase family. {ECO:0000305}.
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DR EMBL; D50617; BAA09180.1; -; Genomic_DNA.
DR EMBL; AY692638; AAT92657.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12379.1; -; Genomic_DNA.
DR PIR; S56194; S56194.
DR RefSeq; NP_014064.1; NM_001183173.1.
DR RefSeq; NP_116594.1; NM_001179906.1.
DR AlphaFoldDB; P0CH63; -.
DR SMR; P0CH63; -.
DR BioGRID; 31086; 49.
DR BioGRID; 35506; 3.
DR STRING; 4932.YFL061W; -.
DR PaxDb; P0CH63; -.
DR EnsemblFungi; YFL061W_mRNA; YFL061W; YFL061W.
DR EnsemblFungi; YNL335W_mRNA; YNL335W; YNL335W.
DR GeneID; 850483; -.
DR GeneID; 855381; -.
DR KEGG; sce:YFL061W; -.
DR KEGG; sce:YNL335W; -.
DR SGD; S000001833; DDI2.
DR VEuPathDB; FungiDB:YFL061W; -.
DR VEuPathDB; FungiDB:YNL335W; -.
DR eggNOG; ENOG502QTPD; Eukaryota.
DR HOGENOM; CLU_079935_0_0_1; -.
DR InParanoid; P0CH63; -.
DR OMA; KMSFEFY; -.
DR BioCyc; YEAST:G3O-30406-MON; -.
DR SABIO-RK; P0CH63; -.
DR PRO; PR:P0CH63; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P0CH63; protein.
DR ExpressionAtlas; P0CH63; baseline and differential.
DR GO; GO:0018820; F:cyanamide hydratase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018890; P:cyanamide metabolic process; IMP:SGD.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR017771; Cyanamide_hydratase_HD.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR TIGRFAMs; TIGR03401; cyanamide_fam; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome; Zinc.
FT CHAIN 1..225
FT /note="Cyanamide hydratase DDI2"
FT /id="PRO_0000202670"
FT DOMAIN 52..162
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 225 AA; 25152 MW; F4890BF675E652B2 CRC64;
MSQYGFVRVP REVEKAIPVV NAPRPRAVVP PPNSETARLV REYAAKELTA PVLNHSLRVF
QYSVAIIRDQ FPAWDLDQEV LYVTCLLHDI ATTDKNMRAT KMSFEYYGGI LSRELVFNAT
GGNQDYADAV TEAIIRHQDL TGTGYITTLG LILQIATTLD NVGSNTDLIH IDTVSAINEQ
FPRLHWLSCF ATVVDTENSR KPWGHTSSLG DDFSKKVICN TFGYN
