ID   PGLRB_NEOFI             Reviewed;         364 AA.
AC   A1DAQ2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=NFIA_095620;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027694; EAW19942.1; -; Genomic_DNA.
DR   RefSeq; XP_001261839.1; XM_001261838.1.
DR   AlphaFoldDB; A1DAQ2; -.
DR   SMR; A1DAQ2; -.
DR   STRING; 36630.CADNFIAP00008561; -.
DR   EnsemblFungi; EAW19942; EAW19942; NFIA_095620.
DR   GeneID; 4588718; -.
DR   KEGG; nfi:NFIA_095620; -.
DR   VEuPathDB; FungiDB:NFIA_095620; -.
DR   eggNOG; ENOG502QTAW; Eukaryota.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   OMA; NYPVQCF; -.
DR   OrthoDB; 601945at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome; Repeat; Secreted; Signal;
KW   Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..29
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393656"
FT   CHAIN           30..364
FT                   /note="Probable endopolygalacturonase B"
FT                   /id="PRO_0000393657"
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        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;  37795 MW;  B000ABC7FCDBD14A CRC64;
     MHFFQSSLVA ATMGAALVAA APAADLETRS SCTFTSTSAL KSGKASCSTI TLHNIAVPAG
     ETLDLTGLKT GTTVVFDGTT TFGYKEWEGP LISASGTSIT IKQNPGGKID CDGARWWDGK
     GGNGGKKKPK FFSAHKLNKS NINGLKVYNI PVHGFSIQSD HLTIKDVLID NSAGTKLGHN
     TDAFDVGSST YITIDGATVY NQDDCLAVNS GEHITFTNGY CNGGHGLSIG SVGGRKNNVV
     NDVTISNSQI INSQNGARIK TVYGATGSVT GVKFQDVSLK GITKYGIVVQ QDYENGKPTG
     NPTNGVKVSD ITFEKVTGSV TSSATDIYIL CGSGSCTNWT WSGNSVTGGK KSSKCKNVPA
     GASC