ID   PGLR2_ASPAW             Reviewed;         362 AA.
AC   Q9P359;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 68.
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;
GN   Name=pgaII; Synonyms=pg2, pgx2;
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-34, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX   PubMed=10993142; DOI=10.1271/bbb.64.1580;
RA   Nagai M., Ozawa A., Katsuragi T., Kawasaki H., Sakai T.;
RT   "Cloning and heterologous expression of gene encoding A polygalacturonase
RT   from Aspergillus awamori.";
RL   Biosci. Biotechnol. Biochem. 64:1580-1587(2000).
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       {ECO:0000269|PubMed:10993142}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. Stable between pH 4.0 and 6.0.
CC         {ECO:0000269|PubMed:10993142};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:10993142};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- INDUCTION: Expression depends of ambient pH (higher at high pHs and
CC       lower at low pHs), probably under the regulation of the pacC
CC       transcription factor. {ECO:0000269|PubMed:10993142}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AB035081; BAA95407.1; -; Genomic_DNA.
DR   PIR; JC7374; JC7374.
DR   AlphaFoldDB; Q9P359; -.
DR   SMR; Q9P359; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28B_ASPAW; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004650; F:polygalacturonase activity; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IDA: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; 5.
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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..27
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393628"
FT   CHAIN           28..362
FT                   /note="Endopolygalacturonase II"
FT                   /id="PRO_0000393629"
FT   REPEAT          156..186
FT                   /note="PbH1 1"
FT   REPEAT          209..229
FT                   /note="PbH1 2"
FT   REPEAT          238..259
FT                   /note="PbH1 3"
FT   REPEAT          267..289
FT                   /note="PbH1 4"
FT   REPEAT          301..322
FT                   /note="PbH1 5"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        203..219
FT                   /evidence="ECO:0000250"
FT   DISULFID        329..334
FT                   /evidence="ECO:0000250"
FT   DISULFID        353..362
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  37625 MW;  E37F4447899C3AAC CRC64;
     MHSFASLLRY GLAAGATLAS ASPIEARDSC TFTTAAAAKA GKAKCSTITL DSIKVPAGTT
     LDLTGLTSGT KVIFEGTTTF DYEDWAGPLI SMSGKDITVT GASGHLINCD GSRWWDGKGT
     SGKKKPKFFY AHGLDSSSIT GLNIKNTPLM AFSVESDDIT LTDITINNAD GDSLGGHNTD
     AFDVGNSVGV NIIKPWVHNQ DDCLAINSGE NIWFTGGTCI GGHGLSIGSV GDRSNNVVKN
     VTIEHSTVSN SENAVRIKTI SGATGSVSEI TYSNIVMSGI SDYGVVIQQD YEDGKPTGKP
     TNGVTITDVK LESVTGTVDS KATDIYLLCG SGSCSDWTWD DVKVTGGKKS SACKNLPSVA
     SC