ID   PGLR2_ASPNG             Reviewed;         362 AA.
AC   P0CU55; P19805;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Endopolygalacturonase II;
DE            Short=EPG-II;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 2;
DE   AltName: Full=Polygalacturonase II;
DE            Short=PG-II;
DE   AltName: Full=Polygalacturonase X2;
DE   Flags: Precursor;
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 [MRNA], AND PROTEIN SEQUENCE OF 28-57.
RC   STRAIN=RH 5344;
RX   PubMed=2400785; DOI=10.1016/0167-4781(90)90130-t;
RA   Ruttowski E., Labitzke R., Khanh N.Q., Loeffler F., Gottschalk M.,
RA   Jany K.-D.;
RT   "Cloning and DNA sequence analysis of a polygalacturonase cDNA from
RT   Aspergillus niger RH5344.";
RL   Biochim. Biophys. Acta 1087:104-106(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RH 5344;
RX   PubMed=1787790; DOI=10.1111/j.1365-2958.1991.tb00782.x;
RA   Ruttkowski E., Khanh N.Q., Wientjes F.J., Gottschalk M.;
RT   "Characterization of a polygalacturonase gene of Aspergillus niger
RT   RH5344.";
RL   Mol. Microbiol. 5:1353-1361(1991).
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; X52903; CAA37085.1; -; mRNA.
DR   EMBL; X54146; CAA38085.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CU55; -.
DR   SMR; P0CU55; -.
DR   STRING; 5061.CADANGAP00011984; -.
DR   VEuPathDB; FungiDB:An15g05370; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1143631; -.
DR   VEuPathDB; FungiDB:ATCC64974_28680; -.
DR   VEuPathDB; FungiDB:M747DRAFT_256960; -.
DR   eggNOG; ENOG502QTAW; 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.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW   Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..27
FT                   /evidence="ECO:0000269|PubMed:2400785"
FT                   /id="PRO_0000442437"
FT   CHAIN           28..362
FT                   /note="Endopolygalacturonase II"
FT                   /id="PRO_0000442438"
FT   REPEAT          156..186
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          238..259
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          267..289
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          301..322
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26214"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P26214"
FT   DISULFID        30..45
FT                   /evidence="ECO:0000250|UniProtKB:P26214"
FT   DISULFID        203..219
FT                   /evidence="ECO:0000250|UniProtKB:P26214"
FT   DISULFID        329..334
FT                   /evidence="ECO:0000250|UniProtKB:P26214"
FT   DISULFID        353..362
FT                   /evidence="ECO:0000250|UniProtKB:P26214"
SQ   SEQUENCE   362 AA;  37513 MW;  AA4AC029DD1E6DEA CRC64;
     MHSFASLLAY GLAASATLAS ASPIEARGSC TFKTAAAAKA GKAGCSTITL DNIEVPAGTT
     LDLTGLTSGT KVIFEGTTTF DYEEWAGPLI SMSGKDITVT GASGHLINCD GARWWDGKGT
     SGKKKPKFFY AHGLDSSSIT GLNIKNTPLM AFSVQADDIT LTDITINNAD GDTLGGHNTD
     AFDVGNSVGV NIIKPWVHNQ DDCLAINSGE NIWFTSGTCI GGHGLSIGSV GGRSNNVVKN
     VTIEHSTVSN SENAVRIKTV SGATGSVSEI TYSNIVMSGI SDYGVVIQQD YEDGKPTGKP
     TNGVTITDVK LESVTGTVDS KATDIYLLCG SGSCSDWTWD DVKVTGGKKS TACKNYPSVA
     SC