ID   PGLRA_ASPKW             Reviewed;         370 AA.
AC   Q8NK99; G7XE19;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 75.
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; ORFNames=AKAW_03292;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RA   Mikami S.;
RT   "Purification and properties of PgaA and PgaB.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AB080269; BAC10596.1; -; Genomic_DNA.
DR   EMBL; DF126452; GAA85178.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NK99; -.
DR   SMR; Q8NK99; -.
DR   STRING; 40384.Q8NK99; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   VEuPathDB; FungiDB:AKAW_03292; -.
DR   eggNOG; ENOG502QST2; Eukaryota.
DR   InParanoid; Q8NK99; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0004650; F:polygalacturonase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS: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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..32
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393639"
FT   CHAIN           33..370
FT                   /note="Probable endopolygalacturonase A"
FT                   /id="PRO_0000393640"
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        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;  38719 MW;  7C2A3D84CDFB6278 CRC64;
     MPSAKPLFCL ATLAGAALAA PAPSRATDFN KRSTCTFTDA ATASESKTSC SDIVLKDITV
     PAGETLNLKD LNDGTTVTFE GTTTWEYEEW DGPLLRISGK DITVTQSSDA VLNGNGAKWW
     DGEGTNGGKT KPKFFYAHDL DDSKISGLYI KNTPVQAISV ESDNLVIEDV TIDNSDGDSE
     GGHNTDGFDI SESTYITITG ATVKNQDDCV AINSGENIYF SGGTCSGGHG LSIGSVGGRD
     DNTVKNVTFI DSTVSDSENG VRIKTVYDAT GTVEDITYSN IQLSGISDYG IVIEQDYENG
     DPTGTPSNGV TISDVTLEDI TGSVDSDAVE IYILCGDGSC TDWTMSGIDI TGGETSSDCE
     NVPSGASCSQ