ID   PGLR_ASPFC              Reviewed;         378 AA.
AC   B0XPA1;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Probable endopolygalacturonase AFUB_016610;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase AFUB_016610;
DE   AltName: Full=Polygalacturonase AFUB_016610;
DE   Flags: Precursor;
GN   ORFNames=AFUB_016610;
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; DS499594; EDP56939.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XPA1; -.
DR   SMR; B0XPA1; -.
DR   EnsemblFungi; EDP56939; EDP56939; AFUB_016610.
DR   VEuPathDB; FungiDB:AFUB_016610; -.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   PhylomeDB; B0XPA1; -.
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; 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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..35
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393690"
FT   CHAIN           36..378
FT                   /note="Probable endopolygalacturonase AFUB_016610"
FT                   /id="PRO_0000393691"
FT   REPEAT          147..169
FT                   /note="PbH1 1"
FT   REPEAT          170..200
FT                   /note="PbH1 2"
FT   REPEAT          201..222
FT                   /note="PbH1 3"
FT   REPEAT          252..273
FT                   /note="PbH1 4"
FT   REPEAT          281..303
FT                   /note="PbH1 5"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        38..56
FT                   /evidence="ECO:0000250"
FT   DISULFID        217..233
FT                   /evidence="ECO:0000250"
FT   DISULFID        345..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..378
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  38425 MW;  BD35BEE28B707357 CRC64;
     MLKLMGSLVL LASAAEVIAS PAAEPVAPST TLEKRAPCTF SGSNGAAAAM ASQKACSTIV
     LSNVAVPAGT TLDLSDLADG TTVTFEGETT WGYQEWSGPL LKISGKNIKV KGASGATLNP
     DGARWWDGQG GNGGKTKPKF FAAHDLTSSS SITDLHILNT PVQAVSINGC DGLTITDITI
     DNSAGDTQGG HNTDAFDIGS SSNIIISGAK VYNQDDCVAV NSGTDITFTG GLCSGGHGLS
     IGSVGGRSDN TVENVSFTNS QVTNSDNGLR IKATKGKTGT IKGVTYSGIT LSSIRKYGIL
     IEQNYDGGDL KGDPTSGIPI TDLTMQNISG KGAVASSGYN IAIVCGSGAC SNWTWKSVEV
     TGGKTYGSCK NVPSVAQC