PGLR1_PENOL
ID PGLR1_PENOL Reviewed; 370 AA.
AC Q9Y834;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Polygalacturonase 1;
DE Short=PG 1;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase 1;
DE Flags: Precursor;
GN Name=PG1;
OS Penicillium olsonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=99116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10802187; DOI=10.1111/j.1574-6968.2000.tb09120.x;
RA Wagner F., Kusserow H., Schaefer W.;
RT "Cloning and targeted disruption of two polygalacturonase genes in
RT Penicillium olsonii.";
RL FEMS Microbiol. Lett. 186:293-299(2000).
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AJ243521; CAB46908.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y834; -.
DR SMR; Q9Y834; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGA28A_PENOL; -.
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..370
FT /note="Polygalacturonase 1"
FT /id="PRO_0000024792"
FT REPEAT 163..194
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 195..216
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 217..237
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 246..267
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 275..297
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..51
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 211..227
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 337..342
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 361..370
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 370 AA; 38063 MW; 35F97F807C09DC1A CRC64;
MRTSILSMLA LGAAAVSAAP AAAAAPAELV ERGSSCTFTS ASAAKAGKKS CSSIVLDNIK
VPAGETLDLS NLKSGTKVTF KGETTFGYKE WKGPLIRFSG KNIEVNGASG HVINGGGASW
WDGKGTNGGK TKPKFFYAHS LDDSTITGLN VKNTPVQGFS VQADNLVLDH ITIDNTDGDK
TNGGHNTDAF DVGESTYITI SNANIKNQDD CLAINSGENI IFTGGTCSGG HGLSIGSVGG
RDDNTVKNVT ISDSTVSNSD NGIRIKTIYK AKGEVADVTF SNIELSNIAK YGIVIEQDYE
NGSPTGKPTT GVPITGLTVE KVTGSVKSSG TDVYILCGSG SCSDWTWSGN KVSGGKTSSK
CKNVPSGASC
