PGLR_SOLLC
ID PGLR_SOLLC Reviewed; 457 AA.
AC P05117; P94004; Q70Y18; Q7DM56;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Polygalacturonase-2;
DE Short=PG;
DE EC=3.2.1.15 {ECO:0000269|PubMed:9701584};
DE AltName: Full=PG-2A;
DE AltName: Full=PG-2B;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN Name=PG2; Synonyms=PG, PG2A, PG2B;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 72-96.
RC STRAIN=cv. Ailsa Craig;
RX PubMed=3786135; DOI=10.1093/nar/14.21.8595;
RA Grierson D., Tucker G.A., Keen J., Ray J., Bird C.R., Schuch W.;
RT "Sequencing and identification of a cDNA clone for tomato
RT polygalacturonase.";
RL Nucleic Acids Res. 14:8595-8603(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RA Sheehy R.E., Pearson J., Brady C.J., Hiatt W.R.;
RT "Molecular characterization of tomato fruit polygalacturonase.";
RL Mol. Gen. Genet. 208:30-36(1987).
RN [3]
RP SEQUENCE REVISION.
RA Hiatt W.R.;
RL Submitted (OCT-1987) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Ailsa Craig;
RX AGRICOLA=IND92000010; DOI=10.1007/BF00017465;
RA Bird C.R., Smith C.J.S., Ray J.A., Moureau P., Bevan M.W., Bird A.S.,
RA Hughes S., Morris P.C., Grierson D., Schuch W.;
RT "The tomato polygalacturonase gene and ripening-specific expression in
RT transgenic plants.";
RL Plant Mol. Biol. 11:651-662(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Ailsa Craig;
RA Bridges I.G., Schuch W.W., Grierson D.;
RT "Anti-sense regulation of plant gene expression.";
RL Patent number EP0271988, 22-JUN-1988.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-115, PROTEIN SEQUENCE OF N-TERMINUS,
RP PROTEIN SEQUENCE OF 72-92, AND GLYCOSYLATION.
RX PubMed=16666031; DOI=10.1104/pp.86.4.1057;
RA DellaPenna D., Bennett A.B.;
RT "In vitro synthesis and processing of tomato fruit polygalacturonase.";
RL Plant Physiol. 86:1057-1063(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
RX PubMed=3405769; DOI=10.1093/nar/16.14.7191;
RA Rose R.E., Houck C.M., Monson E.K., DeJesus C.E., Sheehy R.E., Hiatt W.R.;
RT "The nucleotide sequence of the 5' flanking region of a tomato
RT polygalacturonase gene.";
RL Nucleic Acids Res. 16:7191-7191(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-294.
RC STRAIN=cv. Arka vikas; TISSUE=Fruit;
RA Saiprasad G.V.S.;
RT "Isolation, cloning and characterization of polygalacturonase gene from
RT fruit tissue of Lycopersicum esculentum cv. Arka vikas.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=7449759; DOI=10.1111/j.1432-1033.1980.tb04993.x;
RA Tucker G.A., Robertson N.G., Grierson D.;
RT "Changes in polygalacturonase isoenzymes during the 'ripening' of normal
RT and mutant tomato fruit.";
RL Eur. J. Biochem. 112:119-124(1980).
RN [10]
RP SUBUNIT.
RX PubMed=7227374; DOI=10.1111/j.1432-1033.1981.tb06201.x;
RA Tucker G.A., Robertson N.G., Grierson D.;
RT "The conversion of tomato-fruit polygalacturonase isoenzyme 2 into
RT isoenzyme 1 in vitro.";
RL Eur. J. Biochem. 115:87-90(1981).
RN [11]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
RX PubMed=6617647; DOI=10.1111/j.1432-1033.1983.tb07681.x;
RA Moshrefi M., Luh B.S.;
RT "Carbohydrate composition and electrophoretic properties of tomato
RT polygalacturonase isoenzymes.";
RL Eur. J. Biochem. 135:511-514(1983).
RN [12]
RP INTERACTION WITH GP1, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6489331; DOI=10.1111/j.1432-1033.1984.tb08452.x;
RA Pressey R.;
RT "Purification and characterization of tomato polygalacturonase converter.";
RL Eur. J. Biochem. 144:217-221(1984).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=2152163; DOI=10.2307/3869342;
RA Osteryoung K.W., Toenjes K., Hall B., Winkler V., Bennett A.B.;
RT "Analysis of tomato polygalacturonase expression in transgenic tobacco.";
RL Plant Cell 2:1239-1248(1990).
RN [14]
RP INTERACTION WITH GP1.
RX DOI=10.1007/BF00240897;
RA Pogson B.J., Brady C.J.;
RT "Accumulation of the beta-subunit of polygalacturonase 1 in normal and
RT mutant tomato fruit.";
RL Planta 191:71-78(1993).
RN [15]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=7827495; DOI=10.2307/3869948;
RA Watson C.F., Zheng L., DellaPenna D.;
RT "Reduction of tomato polygalacturonase beta subunit expression affects
RT pectin solubilization and degradation during fruit ripening.";
RL Plant Cell 6:1623-1634(1994).
RN [16]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION BY ETHYLENE.
RX PubMed=12232274; DOI=10.1104/pp.105.4.1189;
RA Zheng L., Watson C.F., DellaPenna D.;
RT "Differential expression of the two subunits of tomato polygalacturonase
RT isoenzyme 1 in wild-type and in tomato fruit.";
RL Plant Physiol. 105:1189-1195(1994).
RN [17]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=12232422; DOI=10.1104/pp.106.4.1461;
RA Moore T., Bennett A.B.;
RT "Tomato fruit polygalacturonase isozyme 1 -- characterization of the beta
RT subunit and its state of assembly in vivo.";
RL Plant Physiol. 106:1461-1469(1994).
RN [18]
RP FUNCTION.
RX PubMed=9747798; DOI=10.1023/a:1006086004262;
RA Cooley M.B., Yoder J.I.;
RT "Insertional inactivation of the tomato polygalacturonase gene.";
RL Plant Mol. Biol. 38:521-530(1998).
RN [19]
RP ENZYME ACTIVITY.
RX PubMed=9701584; DOI=10.1104/pp.117.4.1293;
RA Chun J.-P., Huber D.J.;
RT "Polygalacturonase-mediated solubilization and depolymerization of pectic
RT polymers in tomato fruit cell walls. Regulation By ph and ionic
RT conditions.";
RL Plant Physiol. 117:1293-1299(1998).
RN [20]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15007842; DOI=10.1002/bit.10920;
RA Verlent I., van Loey A., Smout C., Duvetter T., Hendrickx M.E.;
RT "Purified tomato polygalacturonase activity during thermal and high-
RT pressure treatment.";
RL Biotechnol. Bioeng. 86:63-71(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-368.
RX PubMed=14646066; DOI=10.1107/s0907444903018092;
RA Heffron S., Watkins S., Moeller R., Taban A.H., Butowt R., DellaPenna D.,
RA Jurnak F.;
RT "Resolving the space-group ambiguity of crystals of tomato fruit
RT polygalacturonase.";
RL Acta Crystallogr. D 59:2088-2093(2003).
CC -!- FUNCTION: Catalytic subunit of the polygalacturonase isozyme 1 and 2
CC (PG1 and PG2). Acts in concert with the pectinesterase, in the ripening
CC process. Is involved in cell wall metabolism, specifically in
CC polyuronide degradation. The depolymerization and solubilization of
CC cell wall polyuronides mediated by PG2 during ripening seems to be
CC limited by the beta subunit GP1, probably by recruiting PG2 to form
CC PG1. {ECO:0000269|PubMed:2152163, ECO:0000269|PubMed:7827495,
CC ECO:0000269|PubMed:9747798}.
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 Evidence={ECO:0000269|PubMed:9701584};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=276 nm {ECO:0000269|PubMed:15007842,
CC ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
CC ECO:0000269|PubMed:7449759};
CC Note=The ratio of Abs(276)/Abs(260)=1.35. These values are for PG1.;
CC Kinetic parameters:
CC KM=38 uM for polygalacturonic acid (for PG2 at pH 4.6 and 35 degrees
CC Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331,
CC ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
CC KM=75 uM for polygalacturonic acid (for PG1 at pH 4.6 and 35 degrees
CC Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331,
CC ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
CC Vmax=58.8 umol/min/mg enzyme (for PG2 at pH 4.6 and 35 degrees
CC Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331,
CC ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
CC Vmax=7 umol/min/mg enzyme (for PG2 at pH 3.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331,
CC ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
CC Vmax=27.7 umol/min/mg enzyme (for PG1 at pH 4.6 and 35 degrees
CC Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331,
CC ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
CC Vmax=4 umol/min/mg enzyme (for PG1 at pH 3.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331,
CC ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
CC pH dependence:
CC Optimum pH is 4.4-4.8 at 35 degrees Celsius. PG1 is resistant to
CC acidic but not to alkaline conditions, at which PG2 is released from
CC the beta subunit. {ECO:0000269|PubMed:15007842,
CC ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
CC ECO:0000269|PubMed:7449759};
CC Temperature dependence:
CC Optimum temperature is 55-60 degrees Celsius at pH 4.4. PG1 is more
CC thermostable than PG2. {ECO:0000269|PubMed:15007842,
CC ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
CC ECO:0000269|PubMed:7449759};
CC -!- SUBUNIT: Monomer PG2 (isoenzymes PG2A and PG2B). Also forms
CC heterodimers called polygalacturonase 1 (PG1) with the beta subunit
CC GP1. {ECO:0000269|PubMed:12232422, ECO:0000269|PubMed:7227374,
CC ECO:0000269|PubMed:7449759}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:2152163}. Secreted, cell wall
CC {ECO:0000269|PubMed:2152163}. Note=Associated to the cell wall.
CC -!- TISSUE SPECIFICITY: Expressed only in ripening fruits (at protein
CC level). {ECO:0000269|PubMed:12232274, ECO:0000269|PubMed:12232422,
CC ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
CC -!- DEVELOPMENTAL STAGE: PG1 appears when fruits start to be coloured. When
CC fruits are orange, both PG2 and PG1 are present. In fully ripe fruit,
CC mostly PG2 is expressed. {ECO:0000269|PubMed:12232274,
CC ECO:0000269|PubMed:7449759, ECO:0000269|PubMed:7827495}.
CC -!- INDUCTION: By ethylene. {ECO:0000269|PubMed:12232274}.
CC -!- PTM: N-glycosylated. PG2B isozyme has a greater degree of glycosylation
CC than PG2A. {ECO:0000269|PubMed:16666031, ECO:0000269|PubMed:2152163,
CC ECO:0000269|PubMed:6617647}.
CC -!- BIOTECHNOLOGY: The effect of PG can be neutralized by introducing an
CC antisense PG gene by genetic manipulation. The Flavr Savr tomato
CC produced by Calgene (Monsanto) in such a manner has a longer shelf life
CC due to delayed ripening.
CC -!- MISCELLANEOUS: To avoid liquid rheology of tomato juice, temperature
CC and pressure can be increased to inactivate selectively PG2 during the
CC process.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD44521.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X04583; CAA28254.1; -; mRNA.
DR EMBL; X05656; CAA29148.1; -; mRNA.
DR EMBL; X14074; CAA32235.1; -; Genomic_DNA.
DR EMBL; M37304; AAA34178.1; -; Genomic_DNA.
DR EMBL; A15981; CAA01256.1; -; Unassigned_RNA.
DR EMBL; A24194; CAA01720.1; -; Unassigned_DNA.
DR EMBL; M20269; AAA34177.1; -; mRNA.
DR EMBL; X07410; CAA30308.1; -; Genomic_DNA.
DR EMBL; AJ505947; CAD44521.1; ALT_FRAME; mRNA.
DR PIR; A25534; A25534.
DR RefSeq; NP_001234021.1; NM_001247092.2.
DR AlphaFoldDB; P05117; -.
DR SMR; P05117; -.
DR STRING; 4081.Solyc10g080210.1.1; -.
DR Allergome; 6157; Sola l PG.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; P05117; -.
DR PRIDE; P05117; -.
DR EnsemblPlants; Solyc10g080210.2.1; Solyc10g080210.2.1; Solyc10g080210.2.
DR GeneID; 544051; -.
DR Gramene; Solyc10g080210.2.1; Solyc10g080210.2.1; Solyc10g080210.2.
DR KEGG; sly:544051; -.
DR eggNOG; ENOG502QRJW; Eukaryota.
DR HOGENOM; CLU_016031_2_3_1; -.
DR InParanoid; P05117; -.
DR OMA; NNIYARD; -.
DR OrthoDB; 1028572at2759; -.
DR PhylomeDB; P05117; -.
DR BioCyc; MetaCyc:MON-2523; -.
DR Proteomes; UP000004994; Chromosome 10.
DR ExpressionAtlas; P05117; baseline and differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR GO; GO:0009901; P:anther dehiscence; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010047; P:fruit dehiscence; IBA:GO_Central.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Fruit ripening; Genetically modified food;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:16666031"
FT PROPEP 25..71
FT /id="PRO_0000024804"
FT CHAIN 72..444
FT /note="Polygalacturonase-2"
FT /id="PRO_0000024805"
FT PROPEP 445..457
FT /evidence="ECO:0000269|PubMed:16666031"
FT /id="PRO_0000043095"
FT REPEAT 228..255
FT /note="PbH1 1"
FT REPEAT 256..277
FT /note="PbH1 2"
FT REPEAT 309..330
FT /note="PbH1 3"
FT REPEAT 338..359
FT /note="PbH1 4"
FT ACT_SITE 270
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 96
FT /note="E -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="V -> E (in Ref. 8; CAD44521)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="G -> E (in Ref. 8; CAD44521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 50052 MW; 449E4DC36919B074 CRC64;
MVIQRNSILL LIIIFASSIS TCRSNVIDDN LFKQVYDNIL EQEFAHDFQA YLSYLSKNIE
SNNNIDKVDK NGIKVINVLS FGAKGDGKTY DNIAFEQAWN EACSSRTPVQ FVVPKNKNYL
LKQITFSGPC RSSISVKIFG SLEASSKISD YKDRRLWIAF DSVQNLVVGG GGTINGNGQV
WWPSSCKINK SLPCRDAPTA LTFWNCKNLK VNNLKSKNAQ QIHIKFESCT NVVASNLMIN
ASAKSPNTDG VHVSNTQYIQ ISDTIIGTGD DCISIVSGSQ NVQATNITCG PGHGISIGSL
GSGNSEAYVS NVTVNEAKII GAENGVRIKT WQGGSGQASN IKFLNVEMQD VKYPIIIDQN
YCDRVEPCIQ QFSAVQVKNV VYENIKGTSA TKVAIKFDCS TNFPCEGIIM ENINLVGESG
KPSEATCKNV HFNNAEHVTP HCTSLEISED EALLYNY
