ID   PGLRC_ASPNG             Reviewed;         383 AA.
AC   Q12554;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
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;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=1511691; DOI=10.1111/j.1432-1033.1992.tb17161.x;
RA   Bussink H.J.D., Buxton F.P., Fraaye B.A., de Graaff L.H., Visser J.;
RT   "The polygalacturonases of Aspergillus niger are encoded by a family of
RT   diverged genes.";
RL   Eur. J. Biochem. 208:83-90(1992).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; X64356; CAA45707.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12554; -.
DR   SMR; Q12554; -.
DR   STRING; 5061.CADANGAP00004890; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28C_ASPNG; -.
DR   VEuPathDB; FungiDB:An05g02440; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1084547; -.
DR   VEuPathDB; FungiDB:ATCC64974_42870; -.
DR   VEuPathDB; FungiDB:M747DRAFT_362259; -.
DR   eggNOG; ENOG502SHCC; Eukaryota.
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; 4.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cleavage on pair of basic residues;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW   Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..40
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024772"
FT   CHAIN           41..383
FT                   /note="Probable endopolygalacturonase C"
FT                   /id="PRO_0000024773"
FT   REPEAT          175..206
FT                   /note="PbH1 1"
FT   REPEAT          207..228
FT                   /note="PbH1 2"
FT   REPEAT          253..279
FT                   /note="PbH1 3"
FT   REPEAT          287..309
FT                   /note="PbH1 4"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        44..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..239
FT                   /evidence="ECO:0000250"
FT   DISULFID        348..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        372..381
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   383 AA;  40502 MW;  D6A4ED2149FC7A3A CRC64;
     MVRQLILISS LLAAVAVRAP ADPAHPMVTE APDVNLVEKR ATTCTFSGSE GASKASKSKT
     SCSTIYLSDV AVPSGTTLDL SDLNDGTHVI FQGETTFGYE EWEGPLVRVS GTDITVEGES
     DAVLNGDGSR WWDGEGGNGG KTKPKFFYAH DLTSSTIKSI YIENSPVQVF SIDGSTDLTM
     TDITVDNTDG DTDDLAANTD GFDIGESTYI TITGAEIYNQ DDCVAINSGE NIYFSASVCS
     GGHGLSIGSV GGRDDNTVKN VTFYDVNVLK SQQAIRIKTI YGDTGSVSEV TYHEIAFSDA
     TDYGIVIEQN YDDTSKTPTT GVPITDFVLE NIVGTCEDDD CTEVYIACGD GSCSDWTWTG
     VSVTGGSVSD DCLNVPSGIS CDL