ID   PGLR_PENGR              Reviewed;         376 AA.
AC   O93883;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
GN   Name=PGG1;
OS   Penicillium griseoroseum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=84562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCT 6421;
RA   Ribon A.B., Coelho J.L.C., Barros E.G., Araujo E.F.;
RT   "Cloning and characterization of a gene encoding the endopolygalacturonase
RT   of Penicillium griseoroseum.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AF085238; AAC83692.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93883; -.
DR   SMR; O93883; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
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; Glycosidase; Hydrolase;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..376
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024789"
FT   REPEAT          170..208
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          223..243
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          252..273
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          281..303
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          315..360
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        217..233
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        343..348
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        367..376
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   376 AA;  38068 MW;  1EDB1EC56ED56928 CRC64;
     MASSLKLGLI ALLGATAVNA APAAEPVLGT SLLTSRASCT FSGSSGAAEA IKSKTSCSTI
     TLSNVEVPAG TTLDLTGLKS GTTVIFEGTT TFGYKEWEGP LVSVSGTSIT VQGASGAQLN
     GDGARWWDGK GTNGGKTKPK FFYAHSLTNS KIENIYIKNS PVQVFSINGA KELTLSGITV
     DTADGDSNGG HNTDAFDVGS SNGVYITSPI VHNQDDCLAV NSGTNVHFTG AQCTGGHGIS
     IGSVGGRSDN TVDGVTVESC TIKDSDNGVR IKTVYGATGT VQGVTYKDIT LSGIAKYGIV
     IEQDYENGSP TGTPTSGVPI TDLTLDNVHG TVASSGVDTY ILCASGACSD WSWSGVSITG
     GQTSKKCKGI PSGASC