ID   PGLRB_ASPNC             Reviewed;         362 AA.
AC   A2QCV8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=An02g04900;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270009; CAK47667.1; -; Genomic_DNA.
DR   RefSeq; XP_001399628.1; XM_001399591.2.
DR   AlphaFoldDB; A2QCV8; -.
DR   SMR; A2QCV8; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   PaxDb; A2QCV8; -.
DR   EnsemblFungi; CAK47667; CAK47667; An02g04900.
DR   GeneID; 4978979; -.
DR   KEGG; ang:ANI_1_2518024; -.
DR   VEuPathDB; FungiDB:An02g04900; -.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   Proteomes; UP000006706; Chromosome 4R.
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..25
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393652"
FT   CHAIN           26..362
FT                   /note="Probable endopolygalacturonase B"
FT                   /id="PRO_5000219579"
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;  37819 MW;  6CE9660DC8B17B3A CRC64;
     MHFLQNAVVA ATMGAALAAA APLEKRSCTF TSASAAKSGK SSCSTITLDN IAVPAGETLD
     LTGLKKGTTV IFEGETTFGY KEWKGPLISM SGTDITVKQA SGAKINCDGA RWWDGKGSNG
     GKTKPKFFQA HKLDQSSITG LKVYNTPVQG FSILADHLTI TDVTIDNSAG TSKGHNTDAF
     DIGQSTYITI DGATVYNQDD CLAINSGEHI TFTNGYCDGG HGLSIGSIGG RSDNTVNDVT
     ISNSKVLNSQ NGVRIKTIYG KTGTVENVKF EDITLSDISK YGIVVEQDYE NGSPTGTPTN
     GVKVEDITFK KVTGSVKSSG TDIYILCGSG SCSNWTWSGV DVTGGKKSSK CKNVPSGASC
     SD