ID   PGLRB_ASPKA             Reviewed;         362 AA.
AC   Q1HAY5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable endopolygalacturonase B;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase B;
DE   AltName: Full=Polygalacturonase B;
DE   Flags: Precursor;
GN   Name=pgaB; Synonyms=pecB;
OS   Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1069201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kishida M.;
RT   "Polygalacturonase of Aspergillus kawachii.";
RL   Submitted (MAY-2005) 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; AB214906; BAE94655.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1HAY5; -.
DR   SMR; Q1HAY5; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   VEuPathDB; FungiDB:AKAW_00337; -.
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; 6.
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..25
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393650"
FT   CHAIN           26..362
FT                   /note="Probable endopolygalacturonase B"
FT                   /id="PRO_0000393651"
FT   REPEAT          155..184
FT                   /note="PbH1 1"
FT   REPEAT          185..206
FT                   /note="PbH1 2"
FT   REPEAT          207..227
FT                   /note="PbH1 3"
FT   REPEAT          236..257
FT                   /note="PbH1 4"
FT   REPEAT          265..287
FT                   /note="PbH1 5"
FT   REPEAT          299..344
FT                   /note="PbH1 6"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..43
FT                   /evidence="ECO:0000250"
FT   DISULFID        201..217
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..332
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..360
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  37986 MW;  4ABDA5AB291FA672 CRC64;
     MHFLQNAFVA ATMGAAPAAA TPLEKRSCTF TSASAAKSGK SSCSTITFDN IAVPAGETLD
     LTGLKKGTTV IFEGETTFGY KEWKGPLISM SGTDITVKQA SGAKINCDGA RWWDGKGSNG
     GKTKPKFFQA HKLDESSITG LKIYNTPVQG FSILADHLTI TDVTIDDSAG TSKGHNTDAF
     DIGQSTYITI DGATVYNQDD CLAINSGEHI TFTNGYCDGG HGLSIGSIGG RSDNTVNDVT
     ISNSKVVNSQ NGVRIKTIYG KTGTVENVKF EDITLSDISK YGIVVEQDYE NGSPTGTPTN
     GVKVEDITFK KVTGSVKSSG TDIYILCGSG RCSNWTWSGV DVTGGKKSSK CKNVPSGASC
     SD