PGLR_PENJA
ID PGLR_PENJA Reviewed; 371 AA.
AC O42824;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
OS Penicillium janthinellum (Penicillium vitale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5079;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 7719;
RA Ishida Y., Kakibuchi K., Hirao Y., Izumori K.;
RT "Cloning and characterization of a polygalacturonase-encoding gene from
RT Penicillium janthinellum.";
RL J. Ferment. Bioeng. 84:257-260(1997).
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; D79980; BAA24524.1; -; Genomic_DNA.
DR AlphaFoldDB; O42824; -.
DR SMR; O42824; -.
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; 7.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..34
FT /evidence="ECO:0000255"
FT /id="PRO_0000024790"
FT CHAIN 35..371
FT /note="Polygalacturonase"
FT /id="PRO_0000024791"
FT REPEAT 95..117
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 165..195
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 196..217
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 218..238
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 247..268
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 276..298
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT REPEAT 310..355
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 38..53
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 212..228
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 338..343
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 362..371
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 371 AA; 38327 MW; 9E3AD97A1BD2BED5 CRC64;
MPSYLRNLVW ATLAAGLVSA APTPSRVSDL TKKSSSTCTF SSAASASASK SSCSTIVLSN
IEVPAGKTLD LTDLKDGTKV IFEGTTTFGY KEWSGPLIKI SGSDITVEAA DGAVINADGS
RWWDGEGTNG GKTKPKFFYA HSLDDSTISG LNIKNTPVQA FSIQSDNLII DGVTIDNSDG
DENGGHNTDG FDISESTGVT IRNAVVKNQD DCIAINSGQN IYFTGGTCSG GHGLSIGSVG
GRDDNTVKNV TITDSTVTDS ANGVRIKTVY DATGSVSDVT FSDITVSGIT DYGIVIEQDY
ENGSPTGTPT SGVPITDLTV KGITGSVESD AVEVYILCGD DACSDWTWSG VDITSGQTSS
KCENVPSGAS C