ID   PGLR1_ASPTN             Reviewed;         368 AA.
AC   Q0CMU3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Probable endopolygalacturonase I;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 1;
DE   AltName: Full=Polygalacturonase I;
DE            Short=PG-I;
DE   Flags: Precursor;
GN   Name=pgaI; Synonyms=pg1, pga1; ORFNames=ATEG_04991;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476600; EAU34060.1; -; Genomic_DNA.
DR   RefSeq; XP_001214169.1; XM_001214169.1.
DR   AlphaFoldDB; Q0CMU3; -.
DR   SMR; Q0CMU3; -.
DR   STRING; 341663.Q0CMU3; -.
DR   PRIDE; Q0CMU3; -.
DR   EnsemblFungi; EAU34060; EAU34060; ATEG_04991.
DR   GeneID; 4321227; -.
DR   VEuPathDB; FungiDB:ATEG_04991; -.
DR   eggNOG; ENOG502QST2; Eukaryota.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   OMA; EGSRWWD; -.
DR   OrthoDB; 601945at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; 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; Glycosidase; Hydrolase;
KW   Reference proteome; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..31
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393624"
FT   CHAIN           32..368
FT                   /note="Probable endopolygalacturonase I"
FT                   /id="PRO_0000393625"
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   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   368 AA;  38144 MW;  47903A5F6FEA8326 CRC64;
     MHSFQLLGLA ALGSLVAAAP SPSRVSDLTE RSSSCTFTDA AKASSSASSC SSIVLKDIAV
     PAGKTLDLSH VKDGTTITFE GTTTFGYKEW KGPLIRLAGK DITVTMAKGA VIDGEGSRWW
     DGKGTNGGKT KPKFLYAHKL EDSTIKGLNI KNTPVQAISV QANNLHLTDI TIDNSDGDSK
     GGHNTDGFDI SESNGVYISG ANVKNQDDCI AINSGKNIEF TGGTCSGGHG LSIGSIGGRD
     DNTVQGVKIT DSTVTNSDNG IRIKTIVDET GSVSDVTYSN IKLSGIHKKG IVIQQDYKNG
     GPTGKPSNGI PIKDVTVDGI TGSVDSKATP VYILCGSGSC SDWTWKNVKL SGGKSSSECK
     NLPSGVSC