ID   PGLR1_ASPCL             Reviewed;         368 AA.
AC   A1CIV8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=ACLA_052860;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027054; EAW10813.1; -; Genomic_DNA.
DR   RefSeq; XP_001272239.1; XM_001272238.1.
DR   AlphaFoldDB; A1CIV8; -.
DR   SMR; A1CIV8; -.
DR   STRING; 5057.CADACLAP00004327; -.
DR   EnsemblFungi; EAW10813; EAW10813; ACLA_052860.
DR   GeneID; 4703970; -.
DR   KEGG; act:ACLA_052860; -.
DR   VEuPathDB; FungiDB:ACLA_052860; -.
DR   eggNOG; ENOG502QST2; Eukaryota.
DR   HOGENOM; CLU_040116_0_0_1; -.
DR   OMA; EGSRWWD; -.
DR   OrthoDB; 601945at2759; -.
DR   Proteomes; UP000006701; 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; 5.
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; Reference proteome; Repeat; Secreted; Signal;
KW   Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..31
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393617"
FT   CHAIN           32..368
FT                   /note="Probable endopolygalacturonase I"
FT                   /id="PRO_0000393618"
FT   REPEAT          162..192
FT                   /note="PbH1 1"
FT   REPEAT          193..214
FT                   /note="PbH1 2"
FT   REPEAT          244..265
FT                   /note="PbH1 3"
FT   REPEAT          273..295
FT                   /note="PbH1 4"
FT   REPEAT          307..328
FT                   /note="PbH1 5"
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   368 AA;  37860 MW;  03F380892B36D996 CRC64;
     MRSVEILGLA ALGSLVAAAP SPSRVSNSAK KASSCTFTSA AQASKSASGC SEITLDNIAV
     PAGETLDLSH VDDGTTIIFE GTTSFGYKEW KGPLIQFAGT GITVKQNTGA VIDGDGSRWW
     DGKGTNGGKT KPKFMYAHKL RDSTITGLSI KNTPVQAISV QATNLQLTDI TIDNSDGDEN
     GGHNTDAFDI GESNGVYIRG AVVKNQDDCI AINSGENIEF SGGSCSGGHG LSIGSVGGRD
     NNIVKNVTIT DSTISDSDNG VRIKTIYDAT GSVGDVTYSN IKLSNIAKYG IVIEQDYENG
     SPTGTPTTGV PITGLTIDGI TGSVASNAVQ VYILCGDGSC SDWTWKGVDL TGGKKSSKCE
     NVPSGASC