ID   PGLRE_ASPNG             Reviewed;         378 AA.
AC   O42809;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Endopolygalacturonase E;
DE            Short=PGE;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 4;
DE   AltName: Full=Pectinase E;
DE   AltName: Full=Polygalacturonase E;
DE   AltName: Full=Polygalacturonase IV;
DE            Short=PG-IV;
DE   Flags: Precursor;
GN   Name=pgaE;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-59, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=9492270; DOI=10.1046/j.1432-1327.1998.2510072.x;
RA   Parenicova L., Benen J.A.E., Kester H.C.M., Visser J.;
RT   "pgaE encodes a fourth member of the endopolygalacturonase gene family from
RT   Aspergillus niger.";
RL   Eur. J. Biochem. 251:72-80(1998).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.8.;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; Y14386; CAA74744.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42809; -.
DR   SMR; O42809; -.
DR   STRING; 5061.CADANGAP00001406; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28E_ASPNG; -.
DR   VEuPathDB; FungiDB:An01g14670; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1142822; -.
DR   VEuPathDB; FungiDB:ATCC64974_11700; -.
DR   VEuPathDB; FungiDB:M747DRAFT_240324; -.
DR   eggNOG; ENOG502SHCC; Eukaryota.
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   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..39
FT                   /evidence="ECO:0000269|PubMed:9492270"
FT                   /id="PRO_0000024774"
FT   CHAIN           40..378
FT                   /note="Endopolygalacturonase E"
FT                   /id="PRO_0000024775"
FT   REPEAT          103..125
FT                   /note="PbH1 1"
FT   REPEAT          174..204
FT                   /note="PbH1 2"
FT   REPEAT          205..226
FT                   /note="PbH1 3"
FT   REPEAT          256..277
FT                   /note="PbH1 4"
FT   REPEAT          285..307
FT                   /note="PbH1 5"
FT   REPEAT          317..345
FT                   /note="PbH1 6"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        221..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        345..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..378
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  39626 MW;  49DA6728B4BAC6E8 CRC64;
     MVTSSSVIGL TLWAALVSAS PVADPLVTPA PKLEDLEKRA TSCTFSGSEG ASSASKSKTS
     CSTIVLSDVA VPSGTTLDLT DLNDGTHVIF EGETHFGYEE WSGPLVSVSG TDITVTGADG
     AYLNGDGSRW WDGEGSNGGK TKPKFFYAHD LTSSTISGIY IQNSPVQVFS IDGSTYLTME
     DITIDNTDGD DGEAANTDGF DIGDSTYITI TGANVYNQDD CVAVNSGENI YFSGGVCSGG
     HGLSIGSVGG RSDNTVKNVT FYDSDIKSSQ NGVRIKTIYG DTGSVSEVTY KEITLSDITD
     YGIVVEQNYD DTSESPTDGI TIEDFVLDNV QGSVESSGTN IYIVCGSDSC TDWTWTDVDV
     TGGKTSSDCE NVPDDISC