ID   PGLRB_ASPFC             Reviewed;         364 AA.
AC   B0YAH0;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
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; ORFNames=AFUB_084640;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499600; EDP49013.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YAH0; -.
DR   SMR; B0YAH0; -.
DR   EnsemblFungi; EDP49013; EDP49013; AFUB_084640.
DR   VEuPathDB; FungiDB:AFUB_084640; -.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   PhylomeDB; B0YAH0; -.
DR   Proteomes; UP000001699; 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; 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..29
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393644"
FT   CHAIN           30..364
FT                   /note="Probable endopolygalacturonase B"
FT                   /id="PRO_0000393645"
FT   REPEAT          159..188
FT                   /note="PbH1 1"
FT   REPEAT          189..210
FT                   /note="PbH1 2"
FT   REPEAT          211..231
FT                   /note="PbH1 3"
FT   REPEAT          240..261
FT                   /note="PbH1 4"
FT   REPEAT          269..291
FT                   /note="PbH1 5"
FT   REPEAT          303..324
FT                   /note="PbH1 6"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..47
FT                   /evidence="ECO:0000250"
FT   DISULFID        205..221
FT                   /evidence="ECO:0000250"
FT   DISULFID        331..336
FT                   /evidence="ECO:0000250"
FT   DISULFID        355..364
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  37661 MW;  A56743169089B8B8 CRC64;
     MHFFQSSLVA ATMGAALVAA APAADLETRG SCTFTSTSAL KSGKASCSTI TLQNIAVPAG
     ETLDLTGLKA GTTVVFDGTT TFGYKEWEGP LISASGTSIT IKQNPGAKID CDGARWWDGK
     GGNGGKKKPK FFSAHKLNKS NITGLKVYNT PVHGFSIQSD HLTIKDVLLD NSAGTKLGHN
     TDAFDVGSST YITIDGATVY NQDDCLAVNS GEHITFTNGY CNGGHGLSIG SVGGRSNNVV
     NDVTISNSQV INSQNGARIK TVYGATGSVT GVKFQDISLK GITKYGIVVQ QDYENGKPTG
     KPTNGVKVSD ITFEKVTGTV TSSATDIYIL CGSGSCTNWT WSGNSVTGGK KSSSCKNVPA
     GASC