ID   PGLR_PRUPE              Reviewed;         393 AA.
AC   P48979;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Flavorcrest;
RX   PubMed=8029352; DOI=10.1104/pp.105.1.225;
RA   Lester D.R., Speiers J., Orr G., Brady C.J.;
RT   "Peach (Prunus persica) endopolygalacturonase cDNA isolation and mRNA
RT   analysis in melting and nonmelting peach cultivars.";
RL   Plant Physiol. 105:225-231(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; X76735; CAA54150.1; -; mRNA.
DR   PIR; S40123; S40123.
DR   AlphaFoldDB; P48979; -.
DR   SMR; P48979; -.
DR   STRING; 3760.EMJ15083; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   eggNOG; ENOG502QRN7; Eukaryota.
DR   BioCyc; MetaCyc:MON-14862; -.
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; 6.
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;
KW   Fruit ripening; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..393
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024812"
FT   REPEAT          115..136
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          178..204
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          205..226
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          228..248
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          258..279
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          288..309
FT                   /note="PbH1 6"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        221..238
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        349..355
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        376..392
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   393 AA;  41472 MW;  53DCC26944D22BF9 CRC64;
     MANRRSLFSL SLIFVFMINS AIASPLTYNV ASLGAKADGK TDSTKAFLSA WAKACASMNP
     GVIYVPAGTF FLRDVVFSGP CKNNAITFRI AGTLVAPSDY RVIGNAANWI FFHHVNGVTI
     SGGILDGQGT ALWACKACHG ESCPSGATTL GFSDSNNIVV SGLASLNSQM FHIVINDFQN
     VQMQGVRVSR SGNSPNTDGI HVQMSSGVTI LNSKIATGDD CVSIGPGTSN LWIEGVACGP
     GHGISIGSLG KEQEEAGVQN VTVKTVTFSG TQNGLRIKSW GRPSTGFARN ILFQHATMVN
     VENPIVIDQH YCPDNKGCPG QVSGVQISDV TYEDIHGTSA TEVAVKFDCS PKHPCREIKL
     EDVKLTYKNQ AAESSCSHAD GTTEGVVQPT SCL