ID   PGLRA_ASPAW             Reviewed;         370 AA.
AC   Q9P358;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 71.
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, ppas;
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-49, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 38854 / NBRC 4033;
RX   PubMed=10945248; DOI=10.1271/bbb.64.1337;
RA   Nagai M., Ozawa A., Katsuragi T., Sakai T.;
RT   "Purification and characterization of acid-stable protopectinase produced
RT   by Aspergillus awamori in solid-state fermentation.";
RL   Biosci. Biotechnol. Biochem. 64:1337-1344(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:10945248}.
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 2.0. {ECO:0000269|PubMed:10945248};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:10945248};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AB035082; BAA95408.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P358; -.
DR   SMR; Q9P358; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; PGA28A_ASPAW; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0004650; F:polygalacturonase activity; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IDA: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; 6.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW   Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..32
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393633"
FT   CHAIN           33..370
FT                   /note="Endopolygalacturonase A"
FT                   /id="PRO_0000393634"
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..352
FT                   /note="PbH1 6"
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;  38661 MW;  D329CE4AFC197057 CRC64;
     MPSAKPLFCL ATLAGAALAA PAPSRATDFN KRSTCTFTDA ATASESKTSC SDIVLKDITV
     PAGETLNLKD LNDGTTVTFE GTTTWEYEEW DGPLLRISGK DITVTQSSDA VLNGNGAKWW
     DGEGTNGGKT KPKFFYAHDL DDSKISGLYI KNTPVQAISV ESDNLVIEDV TIDNSDGDSE
     GGHNTDGFDI SESTYITITG ATVKNQGDCV AINSGENIYF SGGTCSGGHG LSIGSVGGRD
     DNTVKNVTFI DSTVSDSENG VRIKTVYDAT GTVEDITYSN IQLSGISDYG IVIEQDYENG
     DPTGTPSNGV TISDVTLEDI TGSVDSDAVE IYILCGDGSC TDWTMSGIDI TGGETSSDCE
     NVPSGASCSQ