ID   PGLR_PERAE              Reviewed;         462 AA.
AC   Q02096;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Persea americana (Avocado).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Persea.
OX   NCBI_TaxID=3435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hass; TISSUE=Pericarp;
RX   PubMed=8095163; DOI=10.1007/bf00028802;
RA   Dopico B., Lowe A.L., Wilson I.D., Merodio C., Grierson D.;
RT   "Cloning and characterization of avocado fruit mRNAs and their expression
RT   during ripening and low-temperature storage.";
RL   Plant Mol. Biol. 21:437-449(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hass; TISSUE=Mesocarp;
RX   PubMed=8208850; DOI=10.1104/pp.103.1.289;
RA   Kutsunai S.Y., Lin A.C., Percival F.W., Laties G.G., Christoffersen R.E.;
RT   "Ripening-related polygalacturonase cDNA from avocado.";
RL   Plant Physiol. 103:289-290(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; X66426; CAA47055.1; -; mRNA.
DR   EMBL; L06094; AAA32914.1; -; mRNA.
DR   PIR; S31195; S31195.
DR   AlphaFoldDB; Q02096; -.
DR   SMR; Q02096; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   BioCyc; MetaCyc:MON-14861; -.
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; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..462
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024811"
FT   ACT_SITE        278
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        280..297
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        407..413
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        435..460
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   CONFLICT        182
FT                   /note="S -> I (in Ref. 2; AAA32914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416..419
FT                   /note="YIVG -> ILLE (in Ref. 2; AAA32914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442..462
FT                   /note="LLREGLSTFLFMKRRVHECSY -> TTEGKVYPPSCL (in Ref. 2;
FT                   AAA32914)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  50291 MW;  ABCF068ACCB17A88 CRC64;
     MALTRLLLPI SILWFCFYSS HTILQKDPLL ICVNGDPGFD QRAYPTYFGP ILDEFSSIMG
     FEPSILSLER FNPVGGPETS PDTDISVDDF GARGDGTDDT KAFEKAWKDA CSSGSVLIVP
     ENKNYLLKQI TFSGPCKSDL RVKIRGTIEA SSDQSDWVGH NRKRWIEFED ISNLTLEGGG
     TSNGNGETWW DSSCKRKKSL PCKSAPTALT FRSCKNLIVS DLSIKDSQKM HLSFDKCQDV
     IASNLMVTAP EHSPNTDGIH ITGTQRIHVM NSVIGTGDDC ISIESGSKMV IATNITCGPG
     HGISIGSLGD RNSEAHVSGV LVDGGNLFDT TNGLRIKTWQ GGSGSAKNIK FQNIVMHNVT
     NPIIIDQYYC DSKDPCPEQE SAVKVSNVAY MNIRGTSASE VAVKFDCSKS SPCQGYIVGN
     INLVGNGGKE TTMSCSNIVQ GLLREGLSTF LFMKRRVHEC SY