PGLR1_SCLSC
ID PGLR1_SCLSC Reviewed; 380 AA.
AC Q12708;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Endo-polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN Name=PG1;
OS Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=5180;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SS5;
RX PubMed=8076824; DOI=10.1016/0378-1119(94)90298-4;
RA Reymond P., Deleage G., Rascle C., Fevre M.;
RT "Cloning and sequence analysis of a polygalacturonase-encoding gene from
RT the phytopathogenic fungus Sclerotinia sclerotiorum.";
RL Gene 146:233-237(1994).
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; L12023; AAC14466.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12708; -.
DR SMR; Q12708; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR ABCD; Q12708; 2 sequenced antibodies.
DR VEuPathDB; FungiDB:sscle_16g108170; -.
DR BRENDA; 3.2.1.15; 5625.
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; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..42
FT /evidence="ECO:0000255"
FT /id="PRO_0000024795"
FT CHAIN 43..380
FT /note="Endo-polygalacturonase"
FT /id="PRO_0000024796"
FT REPEAT 178..207
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 208..229
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 230..250
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 259..280
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 288..310
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 322..343
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT ACT_SITE 222
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 46..64
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 224..240
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 350..353
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 371..380
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 380 AA; 37916 MW; 66F7D362A6477B7D CRC64;
MVHILSSALS LLRLGAAVSA APAPAPTAAP NVADALAAVE KRAGSCTFSD PAVPLPAIKS
KASCATIVIS AVAVPSGTTL DLTGLKSGTH VVFEGTTTFG YEEWSGPLVS VSGTDITVTG
ASGSVLDGNG AKYWDGKGTN GGKTKPKFFY AHSLKGKSSI NNVKILNSPV QVFSINSASG
LTLSGITIDN SAGNSLGHNT DAFDVGSSTD ITISGANVQN QDDCLAINSG TGITFTGGTC
SGGHGLSIGS VGGRSDNVVS DVIIESSTVK NSANGVRIKT VLGATGSVSG VTYKDITLSG
ITSYGVVIEQ DYENGSPTGK PTSGVPITGV TLSNVHGTVS SSATNVYVLC AKCSGWTWDV
NVTGGKTSTK CAGLPSGVKC
