PGLR1_COLLN
ID PGLR1_COLLN Reviewed; 363 AA.
AC Q00446;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Endopolygalacturonase 1;
DE EC=3.2.1.15;
DE AltName: Full=Clpg1;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN Name=PG1;
OS Colletotrichum lindemuthianum (Bean anthracnose fungus) (Glomerella
OS lindemuthiana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=290576;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8621072; DOI=10.1016/0378-1119(95)00867-5;
RA Centis S., Dumas B., Fournier J., Marolda M., Esquerre-Tugaye M.T.;
RT "Isolation and sequence analysis of Clpg1, a gene coding for an
RT endopolygalacturonase of the phytopathogenic fungus Colletotrichum
RT lindemuthianum.";
RL Gene 170:125-129(1996).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC the smooth region of the plant cell wall.
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; X89370; CAA61552.1; -; Genomic_DNA.
DR PIR; JC4748; JC4748.
DR AlphaFoldDB; Q00446; -.
DR SMR; Q00446; -.
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; 4.
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; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..26
FT /evidence="ECO:0000255"
FT /id="PRO_0000024784"
FT CHAIN 27..363
FT /note="Endopolygalacturonase 1"
FT /id="PRO_0000024785"
FT REPEAT 188..209
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 210..230
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 239..260
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 268..290
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 29..44
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 204..220
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 330..333
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 352..363
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 363 AA; 36712 MW; A17A60386791B897 CRC64;
MVSYLFVLGA LASVAIASPV PELKARASCT FTDAASAIKG KASCTTIVLN NIAVPAGTTL
DMTGLKSGTH VSFSGKTTFG YKEWEGPLIS FSGSNVVIDG ASGHSIDCQG SRWWDSKGGN
GGKTKPKFFY AHSLKDSTIR GLHTLNTPVQ AFSINGAANL GVYDVSVDNS AGDSAGGHNT
DAFDVGSSTG VYISGADVKN QDDCLAVNSG TNITFTGGTC SGGHGLSIGS VGGRKDNVVK
SVSITNSKII NSDNGVRIKT VAGATGPVSD ITYSGITLSN IAKYGIVIEQ DYENGSPTGK
PTSGVPISGL TLSKISGSVS SSATPVYILC ASCTNWKWSG VSVTGGKKSS KCTGIPSGSG
AAC
