PGLR_PENDI
ID PGLR_PENDI Reviewed; 367 AA.
AC Q9Y718;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN Name=PG1;
OS Penicillium digitatum (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36651;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 9863;
RA Arimoto Y., Arie T., Yamaguchi I.;
RT "Polygalacturonase encoding gene of Penicillium digitatum.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AB015286; BAA77297.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y718; -.
DR SMR; Q9Y718; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
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; 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; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..367
FT /note="Polygalacturonase"
FT /id="PRO_0000024787"
FT REPEAT 161..191
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 192..213
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 214..234
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 243..264
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 272..294
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 34..49
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 208..224
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 334..339
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 358..367
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 367 AA; 37751 MW; 200223ADDD907A4D CRC64;
MRTSFVTMLA LGAAAVSAAP AAPVTDLVER GSSCTFTTAE AAKAGKGSCS TIVLDNIKVP
AGETLDLTKL KSGTQVVFKG ETSFGYKEWT GPLVSFSGSN IHVSGAAGHV INGGGPSWWD
GKGTNGGKKK PKFFYAHHLD DSTISGLNVK NTPVQGFSIL ADRLTLDHIT IDNSEGDAKG
GHNTDAFDVG SSTFITISNA NIKNQDDCLA INSGSNIKFV GGTCSGGHGI SIGSVGLRDN
NIVKDVTISD STVINSDNGV RVKTIYQATG AVSGVTFSNI KLSNIAKYGI VIEQDYENGS
PTGKPTNGVP ISELTIENVT GTLKSSATEV YILCGNGSCK NWKWAGNSLS GGKKSGKCGN
VPAGASC
