ID   PGLR2_PENOL             Reviewed;         380 AA.
AC   Q9Y833;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Polygalacturonase 2;
DE            Short=PG 2;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 2;
DE   Flags: Precursor;
GN   Name=PG2;
OS   Penicillium olsonii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=99116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10802187; DOI=10.1111/j.1574-6968.2000.tb09120.x;
RA   Wagner F., Kusserow H., Schaefer W.;
RT   "Cloning and targeted disruption of two polygalacturonase genes in
RT   Penicillium olsonii.";
RL   FEMS Microbiol. Lett. 186:293-299(2000).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AJ243522; CAB46909.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y833; -.
DR   SMR; Q9Y833; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28B_PENOL; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..38
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024793"
FT   CHAIN           39..380
FT                   /note="Polygalacturonase 2"
FT                   /id="PRO_0000024794"
FT   REPEAT          173..204
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          205..226
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          256..277
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          285..307
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          319..364
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        42..60
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        221..237
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        347..352
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        371..380
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   380 AA;  38653 MW;  2B719D8DC4E23AA6 CRC64;
     MIAGSKLLML GLFGALAVHA LPEPAKAQVT AAPKLEERAT SCTFSGSAGA SSASKSKTAC
     ATIVLSAVAV PSGTTLDLTG LNDGTTVIFE GETTFGYKEW SGPLVSVSGT DITVKGASGA
     TLNGDGSRWW DGKGSNGGKT KPKFFYAHKM FSSTISDIHI VNSPVQVFSI NGATDLTLSG
     ITVDNRDGDT DEGGHNTDAF DVGSSTGITI TGATVYNQDD CLAVNSGTDI TFTGGLCSGG
     HGLSIGSVGG RSNNDVANVI IENSQIQDST NGVRIKTVYE ATGSVKNVTY KDITLSGITK
     YGIVIEQDYE NGSPTGTPTD GVPITDLTLD GVKGTVASSG TNVYILCAEG ACSDWTWDGV
     SVSGGKTSSA CENVPSSASC