ID   PGLRA_ASPPA             Reviewed;         363 AA.
AC   P49575;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Probable endopolygalacturonase A;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase A;
DE   AltName: Full=Polygalacturonase A;
DE   Flags: Precursor;
GN   Name=pgaA; Synonyms=pecA;
OS   Aspergillus parasiticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=5067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / Su-1 / SRRC 143;
RX   PubMed=7883176; DOI=10.1016/0378-1119(94)00749-i;
RA   Cary J.W., Brown R., Cleveland T.E., Whitehead M., Dean R.A.;
RT   "Cloning and characterization of a novel polygalacturonase-encoding gene
RT   from Aspergillus parasiticus.";
RL   Gene 153:129-133(1995).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; U17167; AAA62349.1; -; Genomic_DNA.
DR   EMBL; L23523; AAC37426.1; -; mRNA.
DR   PIR; JC4049; JC4049.
DR   AlphaFoldDB; P49575; -.
DR   SMR; P49575; -.
DR   GlyCosmos; P49575; 1 site, No reported glycans.
DR   VEuPathDB; FungiDB:BDV34DRAFT_211197; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-ARBA.
DR   FunFam; 2.160.20.10:FF:000002; Endopolygalacturonase D; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR050434; Glycosyl_hydrlase_28.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR31884:SF13; ENDOPOLYGALACTURONASE B; 1.
DR   PANTHER; PTHR31884; POLYGALACTURONASE; 1.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SMART; SM00710; PbH1; 6.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   2: Evidence at transcript level;
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_0000024776"
FT   CHAIN           29..363
FT                   /note="Probable endopolygalacturonase A"
FT                   /id="PRO_0000024777"
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;  37506 MW;  55E1D6A3BDA26D4C CRC64;
     MQLLQSSVIA ATVGAALVAA APVELEARDS CTFTSAADAK SGKTSCSTIT LSNIEVPAGE
     TLDLTGLNDG TTVIFSGETT FGYKEWEGPL ISVSGTNIKV QQASGAKIDG DGSRWWDGEG
     GNGGKTKPKF FYAHKLDSSS ITGLQIYNTP VQGFSIQSDN LNITDVTIDN SAGTAEGHNT
     DAFDIGSSTY INIDGATVYN QDDCLAINSG SHITFTNGYC DGGHGLSIGS VGGRSDNTVE
     DVTISNSKVV NSQNGVRIKT VYGATGTVSN VKFEDITLSG ITKYGLVVEQ DYENGSPTGT
     PTNGITVSGI TFEKVTGTVE SDATDIYILC GSGSCTDWTW SGVSITGGKT SSKCENVPTG
     ASC
//