ID   PGLRC_ASPAC             Reviewed;         384 AA.
AC   Q70HJ3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Probable endopolygalacturonase C;
DE            Short=PGC;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 3;
DE   AltName: Full=Pectinase C;
DE   AltName: Full=Polygalacturonase C;
DE   AltName: Full=Polygalacturonase III;
DE            Short=PG-III;
DE   Flags: Precursor;
GN   Name=pgaC; Synonyms=pg3;
OS   Aspergillus aculeatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schnorr K.M., Kauppinen S.;
RT   "Molecular and biochemical characterization of three polygalacturonases
RT   from the filamentous fungus Aspergillus aculeatus.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AJ581482; CAE46195.1; -; mRNA.
DR   AlphaFoldDB; Q70HJ3; -.
DR   SMR; Q70HJ3; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   VEuPathDB; FungiDB:ASPACDRAFT_36925; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0004650; F:polygalacturonase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
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; 4.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..40
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393658"
FT   CHAIN           41..384
FT                   /note="Probable endopolygalacturonase C"
FT                   /id="PRO_0000393659"
FT   REPEAT          176..207
FT                   /note="PbH1 1"
FT   REPEAT          208..229
FT                   /note="PbH1 2"
FT   REPEAT          254..280
FT                   /note="PbH1 3"
FT   REPEAT          288..310
FT                   /note="PbH1 4"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..240
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..354
FT                   /evidence="ECO:0000250"
FT   DISULFID        373..382
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   384 AA;  40004 MW;  BB719077AD58EBEF CRC64;
     MVRQLALACG LLAAVAVQAA PAEPAHPMVT EAPDASLLHK RATTCTFSGS EGASKVSKSK
     TACSTIYLSA LAVPSGTTLD LKDLNDGTHV IFEGETTFGY EEWEGPLVSV SGTDITVEGA
     SGAVLNGDGS RWWDGEGGNG GKTKPKFFAA HDLTSSTIKS IYIENSPVQV FSIDGATDLT
     LTDITIDNTD GDTDDLAANT DGFDIGESTD ITITGAKVYN QDDCVAINSG ENIYFSASVC
     SGGHGLSIGS VGGRDDNTVK NVTFYDVNVL KSQQAIRIKA IYGDTGSISD ITYHEIAFSD
     ATDYGIVIEQ NYDDTSKTPT TGVPITDFTL ENVIGTCADD DCTEVYIACG SGACSDWSWS
     SVSVTGGKVS SKCLNVPSGI SCDL