PGLR_PENEN
ID PGLR_PENEN Reviewed; 378 AA.
AC O59925;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, 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=PEPG1;
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yao C., Conway W.S., Ren R., Sams C.E.;
RT "Cloning and analysis of a gene encoding polygalacturonase in Penicillium
RT expansum.";
RL Submitted (FEB-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF047713; AAC05492.1; -; Genomic_DNA.
DR AlphaFoldDB; O59925; -.
DR SMR; O59925; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR BRENDA; 3.2.1.15; 4613.
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; Glycosidase; Hydrolase;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..378
FT /note="Polygalacturonase"
FT /id="PRO_0000024788"
FT REPEAT 172..203
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 204..225
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 226..246
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 255..276
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 284..306
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT DISULFID 39..57
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 220..236
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 346..352
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 370..378
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 378 AA; 38028 MW; 288518CAF7F6BBD0 CRC64;
MILTRSVVLG FLGSASLALA SPVAELAEGS RLTPRGSACS YSGTSGAAAA IAGKAGCSSI
TLNNVVVPAG TTLDLTGLAS GTKVIFEGTT TFGYKQWAGP LISISGTNIQ VSGASGHLID
GQGSRWWDGE GSNSKTNIKP KFFFAHSLKG SSTITGLNIK DSPVQVFSIS GSSGLTISGV
TIDNKNGDTN SLGHNTDGFD IGDSDSITIT GATVYNQDDC LAINSGTNIV FSGGYCSGGH
GLSIGSVGGR SNNVVETVHI SSTQVVNSQN GVRVKAVSGA TGTIKGVTFQ DITLSGITSQ
GITIRQEYTN SGYTGSPTTG VPITGLTLNN VHGTVTSKGT DITIECGSSA SCSGWTWTKV
AVSGGKADVC KNAPSGTC
