ID   PGLR2_ASPKW             Reviewed;         362 AA.
AC   Q8NK98; G7XU37;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable 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, pgaB; ORFNames=AKAW_08560;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RA   Mikami S.;
RT   "Purification and properties of PgaA and PgaB.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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; AB080270; BAC10597.1; -; Genomic_DNA.
DR   EMBL; DF126473; GAA90446.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NK98; -.
DR   SMR; Q8NK98; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   VEuPathDB; FungiDB:AKAW_08560; -.
DR   InParanoid; Q8NK98; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
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; 5.
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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..27
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393630"
FT   CHAIN           28..362
FT                   /note="Probable endopolygalacturonase II"
FT                   /id="PRO_0000393631"
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"
FT   CONFLICT        127
FT                   /note="K -> T (in Ref. 1; BAC10597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  37604 MW;  793A3C90F4ED26E1 CRC64;
     MHSFASLLAY GLAAGATLAS ASPIEARDSC TFTTAAAAKA GKAKCSTITL DSIKVPAGTT
     LDLTGLTSGT KVIFEGTTTF DYEEWAGPLI 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 SACKNYPSVA
     SC