ID   PGLR_RHIRD              Reviewed;         312 AA.
AC   P27644;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Polygalacturonase;
DE            EC=3.2.1.15;
DE   AltName: Full=PGL;
DE   AltName: Full=Pectinase;
GN   Name=pgl;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A136;
RX   PubMed=1860822; DOI=10.1128/jb.173.16.5110-5120.1991;
RA   Rong L., Karcher S.J., Gelvin S.B.;
RT   "Genetic and molecular analyses of picA, a plant-inducible locus on the
RT   Agrobacterium tumefaciens chromosome.";
RL   J. Bacteriol. 173:5110-5120(1991).
CC   -!- FUNCTION: Seems to regulate the surface properties of the bacterium in
CC       the presence of plant cells or plant cell extracts.
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   -!- INDUCTION: By certain acidic polysaccharides found in carrot root
CC       extract.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; M62814; AAA22102.1; -; Genomic_DNA.
DR   PIR; A40364; A40364.
DR   AlphaFoldDB; P27644; -.
DR   SMR; P27644; -.
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; 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   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Repeat; Secreted.
FT   CHAIN           1..312
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000215228"
FT   REPEAT          80..101
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          116..137
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          143..164
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          222..245
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
SQ   SEQUENCE   312 AA;  32943 MW;  37B03C2EE29F23AB CRC64;
     MALATRATGG AGRRKPVRAR CARGLHLVSC HKTQLLGFTI RNAASWTIHP QGCEDLTAAA
     STIIAPHDSP NTDGFNPESC RNVMISGVRF SVGDDCIAVK AGKRGPDGED DHLAETRGIT
     VRHCLMQPGH GGLVIGSEMS GGVHDVTVED CDMIGTDRGL RLKTGARSGG GMVGNITMRR
     VLLDGVQTAL SANAHYHCDA DGHDDWVQSR NPAPVNDGTP FVDGITVEDV EIRNLAHAAG
     VFLGLPDVPS ATSLSATSPI VSHDPSAVAT PPIMADRVRP MRMRLVFEQA DVVCDDPALL
     NDAPVSISSY FD