ID   PGLR_COCCA              Reviewed;         364 AA.
AC   P26215;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
GN   Name=PGN1;
OS   Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2152162; DOI=10.2307/3869339;
RA   Scott-Craig J.S., Panaccione D.G., Cervone F., Walton J.D.;
RT   "Endopolygalacturonase is not required for pathogenicity of Cochliobolus
RT   carbonum on maize.";
RL   Plant Cell 2:1191-1200(1990).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC       Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC       the smooth region of the plant cell wall.
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; M55979; AAA79885.1; -; Genomic_DNA.
DR   PIR; S28771; S28771.
DR   AlphaFoldDB; P26215; -.
DR   SMR; P26215; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28A_COCCA; -.
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; 6.
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; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..27
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024782"
FT   CHAIN           28..364
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024783"
FT   REPEAT          158..188
FT                   /note="PbH1 1"
FT   REPEAT          189..210
FT                   /note="PbH1 2"
FT   REPEAT          211..231
FT                   /note="PbH1 3"
FT   REPEAT          240..261
FT                   /note="PbH1 4"
FT   REPEAT          269..291
FT                   /note="PbH1 5"
FT   REPEAT          303..348
FT                   /note="PbH1 6"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        205..221
FT                   /evidence="ECO:0000250"
FT   DISULFID        331..336
FT                   /evidence="ECO:0000250"
FT   DISULFID        355..364
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  36597 MW;  501CC8E31F03A304 CRC64;
     MVAYALTSML LSAGALVAAA PSGLDARDGC TFTDAATAIK NKASCSNIVI SGMTVPAGTT
     LDLTGLKSGA TVTFQGTTTF GYKEWEGPLI SVSGTNIKVV GASGHTIDAA GQKWWDGKGS
     NGGKTKPKFF YAHSLTTSSI SGLNIKNTPV QAFSINGVTG LTLDRITIDN SAGDSAGAHN
     TDAFDIGSSS GITISNANIK NQDDCVAINS GSDIHVTNCQ CSGGHGVSIG SVGGRKDNTV
     KGVVVSGTTI ANSDNGVRIK TISGATGSVS DITYENITLK NIAKYGIVIE QDYLNGGPTG
     KPTTGVPITG VTLKNVAGSV TGSGTEIYVL CGKGSCSGWN WSGVSITGGK KSSSCLNVPS
     GASC