ID   PGLRA_ASPFA             Reviewed;         363 AA.
AC   P41749;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Endopolygalacturonase A;
DE            EC=3.2.1.15;
DE   AltName: Full=P2C;
DE   AltName: Full=PGL;
DE   AltName: Full=Pectinase A;
DE   AltName: Full=Polygalacturonase A;
DE   Flags: Precursor;
GN   Name=pgaA; Synonyms=pecA;
OS   Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=ATCC MYA-384 / AF70;
RX   PubMed=7574642; DOI=10.1128/aem.61.9.3316-3322.1995;
RA   Whitehead M.P., Shieh M.T., Cleveland T.E., Cary J.W., Dean R.A.;
RT   "Isolation and characterization of polygalacturonase genes (pecA and pecB)
RT   from Aspergillus flavus.";
RL   Appl. Environ. Microbiol. 61:3316-3322(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.
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   -!- INDUCTION: Expressed in both pectin- and glucose-grown mycelia.
CC       {ECO:0000269|PubMed:7574642}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; U05015; AAA85279.1; -; mRNA.
DR   AlphaFoldDB; P41749; -.
DR   SMR; P41749; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28A_ASPFL; -.
DR   PRIDE; P41749; -.
DR   PHI-base; PHI:88; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
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   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_0000024764"
FT   CHAIN           29..363
FT                   /note="Endopolygalacturonase A"
FT                   /id="PRO_0000024765"
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;  37646 MW;  A6D44A870FD7B30F CRC64;
     MQLLQSSVIA ATVGAALVAA VPVELEARDS CTFTSAADAK SGKTSCSTIT LSNIEVPAGE
     TLDLTGLNDG TTVIFSGETT FGYKEWEGPL ISVSGTNIKV QQASGAKIDG DGSRWWDGKG
     GNGGKTKPKF CYVHKLDSSS ITGLQIYNTP VQGFSIQSDN LNITDVTIDN SAGTAEGHNT
     DAFDVGSSTY INIDGATVYN QDDCLAINSG SHITFTNGYC DGGHGLSIGS VGGRSDNTVE
     DVTISNSKVV NSQNGVRIKT VYDATGTVSN VKFEDITLSG ITKYGLIVEQ DYENGSPTGT
     PTNGIKVSDI TFDKVTGTVE SDATDIYILC GSGSCTDWTW SGVSITGGKT SSKCENVPTG
     ASC