ID   PGLR_PHACE              Reviewed;         367 AA.
AC   O97400; P81523;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Phaedon cochleariae (Mustard beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX   NCBI_TaxID=80249;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA76930.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larval gut {ECO:0000269|PubMed:10612046};
RX   PubMed=10612046; DOI=10.1016/s0965-1748(99)00104-6;
RA   Girard C., Jouanin L.;
RT   "Molecular cloning of cDNAs encoding a range of digestive enzymes from a
RT   phytophagous beetle, Phaedon cochleariae.";
RL   Insect Biochem. Mol. Biol. 29:1129-1142(1999).
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 {ECO:0000305}. Secreted, cell wall
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and adult
CC       gut. {ECO:0000269|PubMed:10612046}.
CC   -!- DEVELOPMENTAL STAGE: Eggs, larvae and adult.
CC       {ECO:0000269|PubMed:10612046}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000255}.
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DR   EMBL; Y17906; CAA76930.1; -; mRNA.
DR   AlphaFoldDB; O97400; -.
DR   SMR; O97400; -.
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   GO; GO:0007586; P:digestion; 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; 2.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   2: Evidence at transcript level;
KW   Cell wall; Cell wall biogenesis/degradation;
KW   Cleavage on pair of basic residues; Digestion; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000316163"
FT   CHAIN           ?..367
FT                   /note="Polygalacturonase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000147328"
FT   REPEAT          187..208
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          240..261
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..42
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        203..219
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        334..339
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        358..367
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   367 AA;  39426 MW;  3059A69AF71E2A76 CRC64;
     MSIRLIAVLS AASIAVTSAT PVADSSCTIS SFDQVASVLA ECTDIVVSNL EVPAGETLNL
     ETKKKGVTIT FEGKTTFAYK EWTGPLLRVK GKAITVVGAK GSVLDGQGQL YWDGKGGNGG
     IKKPKFFKIK ATEGSHFKNI NLLNCPVQVH SIDHSGPLTL SGWNIDVSQG DKDALGHNTD
     GFDINTTDQL TIEDTVVKNQ DDCIAVNQGT NFLFNNLDCS GGHGLSLSVG TSHEIIKNTV
     RNVTFSNSVV RKSRNGIHIK TTYQFRGRYP WRMLTYSNIA MEGIWKYAVN VEQDYKKGKP
     TGIPVGNIPI KGLHLEKVTG TLTGEESTPV YIICADGACS NFNWSGVSFE GASHASNCSY
     VPTGYSC