PGLR_YEAST
ID PGLR_YEAST Reviewed; 361 AA.
AC P47180; D6VWX2; E9P8V0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=PGase SM;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN Name=PGU1; Synonyms=PGL1, PSM1; OrderedLocusNames=YJR153W; ORFNames=J2235;
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=SSM52;
RA Hirose N., Kishida M., Kawasaki H., Sakai T.;
RT "Endo-polygalacturonase gene.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9682473; DOI=10.1111/j.1574-6968.1998.tb13094.x;
RA Blanco P., Sieiro C., Reboredo N.M., Villa T.G.;
RT "Cloning, molecular characterization, and expression of an endo-
RT polygalacturonase-encoding gene from Saccharomyces cerevisiae IM1-8b.";
RL FEMS Microbiol. Lett. 164:249-255(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
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 [6]
RP CHARACTERIZATION.
RC STRAIN=CECT 1389;
RX PubMed=7804908; DOI=10.1139/m94-155;
RA Blanco P., Sieiro C., Diaz A., Villa T.G.;
RT "Production and partial characterization of an endopolygalacturonase from
RT Saccharomyces cerevisiae.";
RL Can. J. Microbiol. 40:974-977(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 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; AB011818; BAA25103.1; -; Genomic_DNA.
DR EMBL; Z49653; CAA89686.1; -; Genomic_DNA.
DR EMBL; AY558092; AAS56418.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08938.1; -; Genomic_DNA.
DR PIR; S57182; S57182.
DR RefSeq; NP_012687.3; NM_001181811.3.
DR AlphaFoldDB; P47180; -.
DR SMR; P47180; -.
DR BioGRID; 33908; 34.
DR STRING; 4932.YJR153W; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGA28A_YEAST; -.
DR PaxDb; P47180; -.
DR PRIDE; P47180; -.
DR EnsemblFungi; YJR153W_mRNA; YJR153W; YJR153W.
DR GeneID; 853618; -.
DR KEGG; sce:YJR153W; -.
DR SGD; S000003914; PGU1.
DR VEuPathDB; FungiDB:YJR153W; -.
DR eggNOG; ENOG502QTAW; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR InParanoid; P47180; -.
DR OMA; GSTIKFM; -.
DR BioCyc; YEAST:YJR153W-MON; -.
DR BRENDA; 3.2.1.15; 984.
DR PRO; PR:P47180; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47180; protein.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0004650; F:polygalacturonase activity; IDA:SGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA:SGD.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..361
FT /note="Polygalacturonase"
FT /id="PRO_0000024797"
FT REPEAT 155..185
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 186..207
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 208..228
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 237..258
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 266..288
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 27..43
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 202..218
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 350..361
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT CONFLICT 23
FT /note="K -> R (in Ref. 5; AAS56418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 37287 MW; A67798529BFB2EFB CRC64;
MISANSLLIS TLCAFAIATP LSKRDSCTLT GSSLSSLSTV KKCSSIVIKD LTVPAGQTLD
LTGLSSGTTV TFEGTTTFQY KEWSGPLISI SGSKISVVGA SGHTIDGQGA KWWDGLGDSG
KVKPKFVKLA LTGTSKVTGL NIKNAPHQVF SINKCSDLTI SDITIDIRDG DSAGGHNTDG
FDVGSSSNVL IQGCTVYNQD DCIAVNSGST IKFMNNYCYN GHGISVGSVG GRSDNTVNGF
WAENNHVINS DNGLRIKTVE GATGTVTNVN FISNKISGIK SYGIVIEGDY LNSKTTGTAT
GGVPISNLVM KDITGSVNST AKRVKILVKN ATNWQWSGVS ITGGSSYSGC SGIPSGSGAS
C
