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   03-AUG-2022, entry version 90.
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; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
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}.
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DR   EMBL; M33692; AAA25931.1; -; Genomic_DNA.
DR   PIR; A44508; A44508.
DR   AlphaFoldDB; P20041; -.
DR   SMR; P20041; -.
DR   STRING; 859657.RPSI07_mp0827; -.
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   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SUPFAM; SSF51126; SSF51126; 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