ID   PGLR_BRANA              Reviewed;         397 AA.
AC   P35337;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Westar; TISSUE=Pollen;
RX   PubMed=8292791; DOI=10.1007/bf00042360;
RA   Robert L.S., Allard S., Gerster J.L., Cass L., Simmonds J.;
RT   "Isolation and characterization of a polygalacturonase gene highly
RT   expressed in Brassica napus pollen.";
RL   Plant Mol. Biol. 23:1273-1278(1993).
CC   -!- FUNCTION: May function in depolymerizing pectin during pollen
CC       development, germination, and tube growth.
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. Secreted, cell wall.
CC   -!- TISSUE SPECIFICITY: Pollen.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; L19879; AAA70402.1; -; mRNA.
DR   PIR; S42549; S42549.
DR   RefSeq; NP_001302495.1; NM_001315566.1.
DR   AlphaFoldDB; P35337; -.
DR   SMR; P35337; -.
DR   Allergome; 1072; Bra n PG.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   GeneID; 106427912; -.
DR   KEGG; bna:106427912; -.
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; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..397
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024801"
FT   REPEAT          169..195
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          196..217
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          219..239
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          249..270
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        212..229
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        341..347
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        370..386
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   397 AA;  42447 MW;  94522440A7134260 CRC64;
     MGSYLGIYTI LVLCLLGYSA NAEVFTAGGP PNSDITAAVL KAFTSACQAP APSQVLIPKG
     DFKLGETVMT GPCKSPIEFT LQGNVKTDGG STQGKDRWVV FEKINGFKLN GGGTFDGEGN
     AAWKANNCHK TFECKKLPIS VRFDFVDNAE IKDVTSLDAK NFHFNVISGK NMTFDNIKII
     APAESPNTDG IHLGRCEGVK ILNTKIATGD DCISVGDGMK NLLIEKVVCG PGHGISVGSL
     GRYGWEQDVT DITVKNCTLE GTSNGLRIKT WPSAACTTTA AGIHFEDIIL NKVSNPILID
     QEYCPWNQCN KNKPSTIKLV DITFRNIRGT SENKDAVKLL CSKGHPCENV EIGDINIEYT
     GPDGPPTFEC TNVTPKLVGA QNPKACVGPV VKAPGKE