ID PGLR_RALSL Reviewed; 529 AA. AC P20041; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 02-SEP-2026, entry version 100. DE RecName: Full=Polygalacturonase; DE Short=PGA; DE EC=3.2.1.15; DE AltName: Full=Pectinase; DE Flags: Precursor; GN Name=pglA; OS Ralstonia solanacearum (Pseudomonas solanacearum). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Ralstonia; OC Ralstonia solanacearum species complex. OX NCBI_TaxID=305; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 22-39. RC STRAIN=AW; RX PubMed=2193922; DOI=10.1128/jb.172.7.3879-3887.1990; RA Huang J., Schell M.A.; RT "DNA sequence analysis of pglA and mechanism of export of its RT polygalacturonase product from Pseudomonas solanacearum."; RL J. Bacteriol. 172:3879-3887(1990). CC -!- FUNCTION: Contributes to the wilt disease production on tomato. 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 -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted. 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; M33692; AAA25931.1; -; Genomic_DNA. DR PIR; A44508; A44508. DR RefSeq; WP_094395200.1; NZ_CP051176.1. DR AlphaFoldDB; P20041; -. DR SMR; P20041; -. 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:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR051801; GH28_Enzymes. DR InterPro; IPR000743; Glyco_hydro_28. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1. DR PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. DR PROSITE; PS00502; POLYGALACTURONASE; 1. PE 1: Evidence at protein level; KW Cell wall biogenesis/degradation; Direct protein sequencing; Glycosidase; KW Hydrolase; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000269|PubMed:2193922" FT CHAIN 22..529 FT /note="Polygalacturonase" FT /id="PRO_0000024761" FT REGION 516..529 FT /note="Required for PGA export across the outer membrane FT and catalytic activity" FT ACT_SITE 305 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052" FT ACT_SITE 331 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052" SQ SEQUENCE 529 AA; 54636 MW; F7438D7C007E401B CRC64; MNHRYTLLAL AAAALSAGAH ATGTSVTAPW GEVAEPSLPA DSAVCKTLSA SITPIKGSVD SVDGNPANSQ PDASRIQSAI DNCPAGQAVK LVKGSAGESG FLSGSLKLKS GVTLWIDTGV TLFASRNPAD YDNGLGTCGT ATTSNDKSCN ALIVARDTAG SGIVGAGAID GRGGSLVTSG PNANRLTWWD IAYLNKTKGL NQQNPRLIQT YNGSAFTLYG VTVQNSPNFH IVTTGTSGVT AWGIKIVTPS LAYAVAGYKC PSGSTPDKVT PATCFTPETV KNTDGFDPGQ STNVVLAYSY INTGDDHVAV KASSGPTRNL LFAHNHFYYG HGLSIGSETN TGVSNMLVTD LTMDGNDSSA GNGLRIKSDA SRGGKVTNIV YDGICMRNVK EPLVFDPFYS SVKGSLYPNF TNIVVKNFHD LGSAKSIKRT MTFLGYKANK QKNPLTITLD NVVFDGTLPA FEGSHYGGPA SPNGVHFTFG GTGPVSFADA IVTSSTTDVT VTGTPGTAAA VDCSKAFVPL KSVAPTSPI //