ID   PGLRA_ASPNG             Reviewed;         370 AA.
AC   Q9P4W4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=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 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], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=10642523; DOI=10.1042/bj3450637;
RA   Parenicova L., Benen J.A., Kester H.C., Visser J.;
RT   "pgaA and pgaB encode two constitutively expressed endopolygalacturonases
RT   of Aspergillus niger.";
RL   Biochem. J. 345:637-644(2000).
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       {ECO:0000269|PubMed:10642523}.
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 4.0. {ECO:0000269|PubMed:10642523};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; Y18804; CAB72125.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P4W4; -.
DR   SMR; Q9P4W4; -.
DR   STRING; 5061.CADANGAP00012918; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28A_ASPNG; -.
DR   VEuPathDB; FungiDB:An16g06990; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1145813; -.
DR   VEuPathDB; FungiDB:ATCC64974_67840; -.
DR   VEuPathDB; FungiDB:M747DRAFT_330493; -.
DR   eggNOG; ENOG502QST2; 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; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..32
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000147349"
FT   CHAIN           33..370
FT                   /note="Endopolygalacturonase A"
FT                   /id="PRO_5000147350"
FT   REPEAT          162..192
FT                   /note="PbH1 1"
FT   REPEAT          193..214
FT                   /note="PbH1 2"
FT   REPEAT          215..235
FT                   /note="PbH1 3"
FT   REPEAT          244..265
FT                   /note="PbH1 4"
FT   REPEAT          273..295
FT                   /note="PbH1 5"
FT   REPEAT          307..328
FT                   /note="PbH1 6"
FT   ACT_SITE        207
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        209..225
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        359..368
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  38735 MW;  158C187F95078BB9 CRC64;
     MPSAKPLFCL ATLAGAALAA PAPSRVSDFT KRSTCTFTDA ATASESKTSC SDIVLKDITV
     PAGETLNLKD LNDGTTVTFE GTTTWEYEEW DGPLLRISGK DITVTQSSDA VLDGNGAKWW
     DGEGTNGGKT KPKFFYAHDL DDSKISGLYI KNTPVQAISV ESDNLVIEDV TIDNSDGDSE
     GGHNTDGFDI SESTYITITG ATVKNQDDCV AINSGENIYF SGGTCSGGHG LSIGSVGGRD
     DNTVKNVTFI DSTVSDSENG VRIKTVYDAT GTVEDITYSN IQLSGISDYG IVIEQDYENG
     DPTGTPSNGV TISDVTLEDI TGSVDSDAVE IYILCGDGSC SDWTMSGIDI TGGETSSDCE
     NVPSGASCDQ