ID   PGLRB_ASPFN             Reviewed;         363 AA.
AC   B8N7Z8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=AFLA_105920;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963475; EED53217.1; -; Genomic_DNA.
DR   RefSeq; XP_002376463.1; XM_002376422.1.
DR   AlphaFoldDB; B8N7Z8; -.
DR   SMR; B8N7Z8; -.
DR   STRING; 5059.CADAFLAP00004328; -.
DR   EnsemblFungi; EED53217; EED53217; AFLA_105920.
DR   VEuPathDB; FungiDB:AFLA_105920; -.
DR   eggNOG; ENOG502QTAW; Eukaryota.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   OMA; GSTIKFM; -.
DR   Proteomes; UP000001875; 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..28
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393646"
FT   CHAIN           29..363
FT                   /note="Probable endopolygalacturonase B"
FT                   /id="PRO_0000393647"
FT   REPEAT          158..187
FT                   /note="PbH1 1"
FT   REPEAT          188..209
FT                   /note="PbH1 2"
FT   REPEAT          210..230
FT                   /note="PbH1 3"
FT   REPEAT          239..260
FT                   /note="PbH1 4"
FT   REPEAT          268..290
FT                   /note="PbH1 5"
FT   REPEAT          302..347
FT                   /note="PbH1 6"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        204..220
FT                   /evidence="ECO:0000250"
FT   DISULFID        330..335
FT                   /evidence="ECO:0000250"
FT   DISULFID        354..363
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  37662 MW;  D7BA06F6CA00E9A0 CRC64;
     MQLLQSSVIA ATVGAALVAA VPVELEARDS CTFTSAADAK SGKTSCSTIT LSNIEVPAGE
     TLDLTGLNDG TTVIFSGETT FGYKEWEGPL ISVSGTNIKV QQASGAKIDG DGSRWWDGKG
     GNGGKTKPKF FYAHKLDSSS ITGLQIYNTP VQGFSIQSDN LNITDVTIDN SAGTAEGHNT
     DAFDVGSSTY INIDGATVYN QDDCLAINSG SHITFTNGYC DGGHGLSIGS VGGRSDNTVE
     DVTISNSKVV NSQNGVRIKT VYDATGTVSN VKFEDITLSG ITKYGLIVEQ DYENGSPTGT
     PTNGIKVSDI TFDKVTGTVE SDATDIYILC GSGSCTDWTW SGVSITGGKT SSKCENVPTG
     ASC