ID   PGLR_OENOR              Reviewed;         362 AA.
AC   P24548;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Exopolygalacturonase;
DE            Short=ExoPG;
DE            EC=3.2.1.67;
DE   AltName: Full=Galacturan 1,4-alpha-galacturonidase;
DE   AltName: Full=Pectinase;
DE   Flags: Fragment;
OS   Oenothera organensis (Evening primrose).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX   NCBI_TaxID=3945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pollen;
RX   PubMed=2152116; DOI=10.2307/3869141;
RA   Brown S.M., Crouch M.L.;
RT   "Characterization of a gene family abundantly expressed in Oenothera
RT   organensis pollen that shows sequence similarity to polygalacturonase.";
RL   Plant Cell 2:263-274(1990).
CC   -!- FUNCTION: May function in depolymerizing pectin during pollen
CC       development, germination, and tube growth. Acts as an exo-
CC       polygalacturonase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC         galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC         Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, cell wall
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Pollen tubes growing through the style during
CC       pollination.
CC   -!- DEVELOPMENTAL STAGE: Accumulates late in pollen development and/or
CC       during germination and tube growth.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   PIR; JQ0992; JQ0992.
DR   AlphaFoldDB; P24548; -.
DR   SMR; P24548; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
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; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Repeat; Secreted.
FT   CHAIN           <1..362
FT                   /note="Exopolygalacturonase"
FT                   /id="PRO_0000215229"
FT   REPEAT          138..164
FT                   /note="PbH1 1"
FT   REPEAT          165..186
FT                   /note="PbH1 2"
FT   REPEAT          188..208
FT                   /note="PbH1 3"
FT   REPEAT          218..239
FT                   /note="PbH1 4"
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   362 AA;  38207 MW;  0AD6F45B5518B947 CRC64;
     DSTQALTTAW KEACASASPS TILVPKGNFA VGLITLEGPC KSSIGLQLQG TLKAPADPSK
     IKGLGWINLN KIDLLTIFGG GVFDGQGKSA WVQNDCHKNG PICKTLSMNL RLYAVTNSIL
     RDVTTLDSKN FHVNVIGCKN LTFERFKISA AETSINTDGI HIGRSDGVNI INTEIKTGDD
     CISLGDGSKN INITNITCGP GHGISVGSLG RYKNEESVVG IYVKNCTITG SQNGVRIKTW
     PKSEPGEASE MHFQDITMNS VGTPILIDQG YCPYNQCTAE VPSSVKLSKI SFKNIKGTST
     TKEAVKLVCS KSFPCNGVEL ADIDLTYSGK GGPATSVCEN IKPTIKGKQI PAICSGSAAK
     AA