ID   PGLR_ACTDE              Reviewed;         467 AA.
AC   P35336;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Actinidia deliciosa (Kiwi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Actinidiaceae; Actinidia.
OX   NCBI_TaxID=3627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Hayward;
RX   PubMed=8029342; DOI=10.1104/pp.103.2.669;
RA   Atkinson R.G., Gardner R.C.;
RT   "A polygalacturonase gene from kiwifruit (Actinidia deliciosa).";
RL   Plant Physiol. 103:669-670(1993).
CC   -!- FUNCTION: Acts in concert with the pectinesterase, in the ripening
CC       process. Is involved in cell wall metabolism, specifically in
CC       polyuronide degradation.
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   -!- DEVELOPMENTAL STAGE: In ripening fruit.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; L12019; AAC14453.1; -; Genomic_DNA.
DR   AlphaFoldDB; P35336; -.
DR   SMR; P35336; -.
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:0009835; P:fruit ripening; 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; Fruit ripening; Glycoprotein;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..467
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024798"
FT   ACT_SITE        283
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   467 AA;  50776 MW;  5A9A61483C028B7A CRC64;
     MALQRRFFQF VIITLLIPSF ILGYTSAVHE DPPHDYHLEE YGYDFKAYPS YITTIGDNDF
     GSSMSHENGI FGLRKVDYGM DRVLDASKTV NVDDFGAKGD GRDDTKAFEK AWKAACSSTS
     SAVLLVPKKN YLVRPISFSG PCKSGLTMQI YGTIEASDDR SDYRKDGRHW LVFDSVQNLR
     VEGGGTINGN GKIWWQNSCK TNKALPCKDA PTALTFYKSK HVIVKNLKIE NAQQIHVSFD
     NCVNVQASNL MVTAPENSPN TDGIHVTGTQ NIHISSCVIG TGDDCISIVN GSRKVRVNDI
     TCGPGHGISI GSLGYGNSEA HVSDVVVNGA KLCGTTNGVR IKTWQGGSGS ASNIKFQNVE
     MHNVENPIII DQNYCDQDKP CQEQSSAVQV KNVVYQNIKG TCASNVAITF DCSKRFPCQG
     IVLEDVDLEI EGGAAAKALC NNVELSETGV VSPHCQEEGG EEEEEAS