ID H6W9D2_9HELO Unreviewed; 310 AA. AC H6W9D2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 24-JAN-2024, entry version 28. DE RecName: Full=endo-polygalacturonase {ECO:0000256|ARBA:ARBA00012736}; DE EC=3.2.1.15 {ECO:0000256|ARBA:ARBA00012736}; DE Flags: Fragment; OS Botryotinia calthae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botryotinia. OX NCBI_TaxID=38488 {ECO:0000313|EMBL:AFA52636.1}; RN [1] {ECO:0000313|EMBL:AFA52636.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMK753 {ECO:0000313|EMBL:AFA52636.1}; RX PubMed=22253834; DOI=10.1371/journal.pone.0029943; RA Andrew M., Barua R., Short S.M., Kohn L.M.; RT "Evidence for a common toolbox based on necrotrophy in a fungal lineage RT spanning necrotrophs, biotrophs, endophytes, host generalists and RT specialists."; RL PLoS ONE 7:E29943-E29943(2012). 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 Evidence={ECO:0000256|ARBA:ARBA00034074}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}. 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; JQ035920; AFA52636.1; -; Genomic_DNA. DR AlphaFoldDB; H6W9D2; -. DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro. 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; Single-stranded right-handed beta-helix, Pectin lyase-like; 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 PANTHER; PTHR31884; POLYGALACTURONASE; 1. DR PANTHER; PTHR31884:SF1; POLYGALACTURONASE; 1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR SMART; SM00710; PbH1; 6. DR SUPFAM; SSF51126; Pectin lyase-like; 1. DR PROSITE; PS00502; POLYGALACTURONASE; 1. PE 3: Inferred from homology; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT ACT_SITE 205 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10052" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AFA52636.1" FT NON_TER 310 FT /evidence="ECO:0000313|EMBL:AFA52636.1" SQ SEQUENCE 310 AA; 31349 MW; 2C7A1AA010347C04 CRC64; KRATTCTFSG SGGASSASKS KTSCSTIILS ALAVPSGTTL DLTGLTKGTT VIFEGITTFG YEEWSGPLVS VSGTDITVTQ TTGAYLDGGG ASYWDGDGSN GGKTKPKFFY AHSLISSTIE NLYFLNPPVQ VMSINSATDL TVSGVTINAQ DGDTGSLGAN TDGFDIGSST TVTITGANVY NQDDCVAINS GTGITFSGGV CSGGHGLSIG SVGGRDDNIV ETVLFENSEI KASQNGIRIK TISGDTGTVS GITYSGITLS GITDYGIVVN QAYDGTSGEP TNGVAISKFI LENISGTVES TATNILVECG //