ID   PGLR1_ASPFN             Reviewed;         367 AA.
AC   B8N8M2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable endopolygalacturonase I;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 1;
DE   AltName: Full=Polygalacturonase I;
DE            Short=PG-I;
DE   Flags: Precursor;
GN   Name=pgaI; Synonyms=pg1, pga1; ORFNames=AFLA_108160;
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; EED53441.1; -; Genomic_DNA.
DR   RefSeq; XP_002376687.1; XM_002376646.1.
DR   AlphaFoldDB; B8N8M2; -.
DR   SMR; B8N8M2; -.
DR   STRING; 5059.CADAFLAP00004552; -.
DR   EnsemblFungi; EED53441; EED53441; AFLA_108160.
DR   VEuPathDB; FungiDB:AFLA_108160; -.
DR   eggNOG; ENOG502QTAW; Eukaryota.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   OMA; EGSRWWD; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; 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..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..30
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393619"
FT   CHAIN           31..367
FT                   /note="Probable endopolygalacturonase I"
FT                   /id="PRO_0000393620"
FT   REPEAT          161..191
FT                   /note="PbH1 1"
FT   REPEAT          192..213
FT                   /note="PbH1 2"
FT   REPEAT          214..234
FT                   /note="PbH1 3"
FT   REPEAT          243..264
FT                   /note="PbH1 4"
FT   REPEAT          272..294
FT                   /note="PbH1 5"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..49
FT                   /evidence="ECO:0000250"
FT   DISULFID        208..224
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..339
FT                   /evidence="ECO:0000250"
FT   DISULFID        358..367
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  37798 MW;  98951FF0FC242576 CRC64;
     MHFQLLGLAA LGSLAAAAPA PSRTSELVER GSSCTFTSAA QASASAKSCS NIVLKNIAVP
     AGETLDLSKA KDGATITFEG TTTFGYKEWK GPLIRFGGNK ITVTQAAGAV IDGQGSRWWD
     GKGTNGGKTK PKFIYAHKLQ SSTIKGLHVK NSPVQVFSVQ GNDVHLTDIT IDNSDGDNNG
     GHNTDAFDVS ESNGVYITGA NVKNQDDCLA INSGENIEFT GATCSGGHGI SIGSIGNRDS
     NTVKNVKVAD STVVDSDNGI RIKTISGATG SVSGVTYENI TLKNIKKNGI VIEQDYKNGG
     PTGKPTTGVP ITDLTVNGVT GSVASKATPV YILCGKGSCS DWTWKGVSIS GGKKSDKCQN
     IPSGASC