ID   PGLR_MALDO              Reviewed;         460 AA.
AC   P48978;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Golden Delicious;
RX   PubMed=7972500; DOI=10.1104/pp.105.4.1437;
RA   Atkinson R.G.;
RT   "A cDNA clone for endopolygalacturonase from apple.";
RL   Plant Physiol. 105:1437-1438(1994).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; L27743; AAA74452.1; -; mRNA.
DR   PIR; T17011; T17011.
DR   AlphaFoldDB; P48978; -.
DR   SMR; P48978; -.
DR   BioCyc; MetaCyc:MONOMER-14863; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009901; P:anther dehiscence; IEA:UniProtKB-ARBA.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009830; P:cell wall modification involved in abscission; IEA:UniProtKB-ARBA.
DR   GO; GO:0010047; P:fruit dehiscence; IEA:UniProtKB-ARBA.
DR   FunFam; 2.160.20.10:FF:000028; Polygalacturonase QRT2; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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   PANTHER; PTHR31375; -; 1.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SMART; SM00710; PbH1; 6.
DR   SUPFAM; SSF51126; Pectin lyase-like; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..460
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024809"
FT   ACT_SITE        292
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   460 AA;  49404 MW;  13E99A7A049F4FCE CRC64;
     MALKTQLLWS FVVVFVVSFS TTSCSGSSFQ EVNALHSYVD HVDDKESGYN SRAYPSYTDT
     IEGLKVMELI RPRTQLFSSR KLNTITGGIA TSSAPAKTIS VDDFGAKGNG ADDTQAFVKA
     WKAACSSSGA MVLVVPQKNY LVRPIEFSGP CKSQLTLQIY GTIEASEDRS IYKDIDHWLI
     FDNVQNLLVV GPGTINGNGN IWWKNSCKIK PQPPCGTYAP TAVTFNRCNN LVVKNLNIQD
     AQQIHVIFQN CINVQASCLT VTAPEDSPNT DGIHVTNTQN ITISSSVIGT GDDCISIVSG
     SQRVQATDIT CGPGHGISIG SLGEDGSEDH VSGVFVNGAK LSGTSNGLRI KTWKGGSGSA
     TNIVFQNVQM NDVTNPIIID QNYCDHKTKD CKQQKSAVQV KNVLYQNIRG TSASGDAITL
     NCSQSVPCQG IVLQSVQLQN GRAECNNVQP AYKGVVSPRC
//