CPD1_YEAST
ID CPD1_YEAST Reviewed; 239 AA.
AC P53314; D6VV27;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000303|PubMed:7929175};
DE Short=CPDase {ECO:0000303|PubMed:7929175};
DE EC=3.1.4.37 {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
GN Name=CPD1 {ECO:0000303|PubMed:7929175}; OrderedLocusNames=YGR247W;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9133742;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<373::aid-yea82>3.0.co;2-v;
RA Feroli F., Carignani G., Pavanello A., Guerreiro P., Azevedo D.,
RA Rodrigues-Pousada C., Melchioretto P., Panzeri L., Agostoni Carbone M.L.;
RT "Analysis of a 17.9 kb region from Saccharomyces cerevisiae chromosome VII
RT reveals the presence of eight open reading frames, including BRF1
RT (TFIIIB70) and GCN5 genes.";
RL Yeast 13:373-377(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7929175; DOI=10.1016/s0021-9258(17)31479-5;
RA Culver G.M., Consaul S.A., Tycowski K.T., Filipowicz W., Phizicky E.M.;
RT "tRNA splicing in yeast and wheat germ. A cyclic phosphodiesterase
RT implicated in the metabolism of ADP-ribose 1',2'-cyclic phosphate.";
RL J. Biol. Chem. 269:24928-24934(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-39; THR-41; HIS-150 AND SER-152.
RX PubMed=10734185; DOI=10.1093/nar/28.8.1676;
RA Nasr F., Filipowicz W.;
RT "Characterization of the Saccharomyces cerevisiae cyclic nucleotide
RT phosphodiesterase involved in the metabolism of ADP-ribose 1',2'-cyclic
RT phosphate.";
RL Nucleic Acids Res. 28:1676-1683(2000).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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: Involved in the metabolism of ADP-ribose 1',2'-cyclic
CC phosphate which is produced as a consequence of tRNA splicing.
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-
CC phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37;
CC Evidence={ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.97 mM for adenosine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC KM=14.29 mM for guanosine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC KM=12.18 mM for cytidine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC KM=8.91 mM for uridine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC KM=0.37 mM for ADP-ribose 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC KM=0.33 mM for ribose 1,3-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC Vmax=353 umol/min/mg enzyme toward adenosine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC Vmax=390 umol/min/mg enzyme toward guanosine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC Vmax=598 umol/min/mg enzyme toward cytidine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC Vmax=296 umol/min/mg enzyme toward uridine 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC Vmax=61 umol/min/mg enzyme toward ADP-ribose 1',2'-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC Vmax=0.02 umol/min/mg enzyme toward ribose 1,3-cyclic phosphate
CC {ECO:0000269|PubMed:10734185, ECO:0000269|PubMed:7929175};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CPD1 family.
CC {ECO:0000305}.
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DR EMBL; Y07703; CAA68969.1; -; Genomic_DNA.
DR EMBL; Z73032; CAA97276.1; -; Genomic_DNA.
DR EMBL; AY558381; AAS56707.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08338.1; -; Genomic_DNA.
DR PIR; S64573; S64573.
DR RefSeq; NP_011763.1; NM_001181376.1.
DR AlphaFoldDB; P53314; -.
DR BioGRID; 33498; 50.
DR DIP; DIP-5558N; -.
DR IntAct; P53314; 1.
DR STRING; 4932.YGR247W; -.
DR MaxQB; P53314; -.
DR PaxDb; P53314; -.
DR PRIDE; P53314; -.
DR TopDownProteomics; P53314; -.
DR EnsemblFungi; YGR247W_mRNA; YGR247W; YGR247W.
DR GeneID; 853162; -.
DR KEGG; sce:YGR247W; -.
DR SGD; S000003479; CPD1.
DR VEuPathDB; FungiDB:YGR247W; -.
DR eggNOG; ENOG502RY6J; Eukaryota.
DR HOGENOM; CLU_088289_0_0_1; -.
DR OMA; FEPHITI; -.
DR BioCyc; MetaCyc:YGR247W-MON; -.
DR BioCyc; YEAST:YGR247W-MON; -.
DR SABIO-RK; P53314; -.
DR PRO; PR:P53314; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53314; protein.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IDA:SGD.
DR GO; GO:0009187; P:cyclic nucleotide metabolic process; IDA:SGD.
DR InterPro; IPR012386; Cyclic-nucl_3Pdiesterase.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR PANTHER; PTHR28141; PTHR28141; 1.
DR Pfam; PF07823; CPDase; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Hydrolase; Reference proteome.
FT CHAIN 1..239
FT /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT /id="PRO_0000202859"
FT ACT_SITE 39
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P16330"
FT ACT_SITE 150
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P16330"
FT MUTAGEN 39
FT /note="H->A: Abolishes cyclic nucleotide phosphodiesterase
FT activity."
FT /evidence="ECO:0000269|PubMed:10734185"
FT MUTAGEN 41
FT /note="T->A: Reduces strongly cyclic nucleotide
FT phosphodiesterase activity."
FT /evidence="ECO:0000269|PubMed:10734185"
FT MUTAGEN 150
FT /note="H->A: Abolishes cyclic nucleotide phosphodiesterase
FT activity."
FT /evidence="ECO:0000269|PubMed:10734185"
FT MUTAGEN 152
FT /note="S->A: Reduces strongly cyclic nucleotide
FT phosphodiesterase activity."
FT /evidence="ECO:0000269|PubMed:10734185"
SQ SEQUENCE 239 AA; 26732 MW; DE38A74FAD0E3A55 CRC64;
MAIALWYCPP QGSVAYETLQ MLIFSFQTLF PDSPVFEPHV TVTSHLVCNS KDDVNKILTS
CVAAIQSIRS HQTAKKGRKG QVSHAVAAPL VSFNGCSVGK QYFKKIVLEC NKNKILYGVA
QVMREMYVEI DPETRSSRAA TWVHEEFHPH VSLLYSDIHP VSQASLRVVQ QRIEDALDVQ
LVPREKRKGS GNADGSNEVQ MRWDFDVSSS LSWNIPGTFK VVNCVGPVQE WEVLGRVDV
