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UniProtKB/Swiss-Prot entry P05117


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PGLR_SOLLC
Primary accession number P05117
Secondary accession numbers P94004 Q70Y18 Q7DM56
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 81)
Name and origin of the protein
Protein name Polygalacturonase-2 [Precursor]
Synonyms PG
EC 3.2.1.15
PG-2A
PG-2B
Pectinase
Gene name
Name: PG2
Synonyms: PG, PG2A, PG2B
From
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum; Lycopersicon.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 72-96.
STRAIN=cv. Ailsa Craig;
DOI=10.1093/nar/14.21.8595; PubMed=3786135 [NCBI, ExPASy, EBI, Israel, Japan]
Grierson D., Tucker G.A., Keen J., Ray J., Bird C.R., Schuch W.;
"Sequencing and identification of a cDNA clone for tomato polygalacturonase.";
Nucleic Acids Res. 14:8595-8603(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
Sheehy R.E., Pearson J., Brady C.J., Hiatt W.R.;
"Molecular characterization of tomato fruit polygalacturonase.";
Mol. Gen. Genet. 208:30-36(1987).
[3]
SEQUENCE REVISION.
Hiatt W.R.;
Submitted (OCT-1987) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Ailsa Craig;
DOI=10.1007/BF00017465; AGRICOLA=IND92000010
Bird C.R., Smith C.J.S., Ray J.A., Moureau P., Bevan M.W., Bird A.S., Hughes S., Morris P.C., Grierson D., Schuch W.;
"The tomato polygalacturonase gene and ripening-specific expression in transgenic plants.";
Plant Mol. Biol. 11:651-662(1988).
[5]
NUCLEOTIDE SEQUENCE.
STRAIN=cv. Ailsa Craig;
Bridges I.G., Schuch W.W., Grierson D.;
"Anti-sense regulation of plant gene expression.";
Patent number EP0271988, 22-JUN-1988.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-115, PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN SEQUENCE OF 72-92, AND GLYCOSYLATION.
PubMed=16666031 [NCBI, ExPASy, EBI, Israel, Japan]
DellaPenna D., Bennett A.B.;
"In vitro synthesis and processing of tomato fruit polygalacturonase.";
Plant Physiol. 86:1057-1063(1988).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
DOI=10.1093/nar/16.14.7191; PubMed=3405769 [NCBI, ExPASy, EBI, Israel, Japan]
Rose R.E., Houck C.M., Monson E.K., DeJesus C.E., Sheehy R.E., Hiatt W.R.;
"The nucleotide sequence of the 5' flanking region of a tomato polygalacturonase gene.";
Nucleic Acids Res. 16:7191-7191(1988).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 96-294.
STRAIN=cv. Arka vikas;
TISSUE=Fruit;
Saiprasad G.V.S.;
"Isolation, cloning and characterization of polygalacturonase gene from fruit tissue of Lycopersicum esculentum cv. Arka vikas.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[9]
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DEVELOPMENTAL STAGE.
PubMed=7449759 [NCBI, ExPASy, EBI, Israel, Japan]
Tucker G.A., Robertson N.G., Grierson D.;
"Changes in polygalacturonase isoenzymes during the 'ripening' of normal and mutant tomato fruit.";
Eur. J. Biochem. 112:119-124(1980).
[10]
SUBUNIT.
PubMed=7227374 [NCBI, ExPASy, EBI, Israel, Japan]
Tucker G.A., Robertson N.G., Grierson D.;
"The conversion of tomato-fruit polygalacturonase isoenzyme 2 into isoenzyme 1 in vitro.";
Eur. J. Biochem. 115:87-90(1981).
[11]
BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
PubMed=6617647 [NCBI, ExPASy, EBI, Israel, Japan]
Moshrefi M., Luh B.S.;
"Carbohydrate composition and electrophoretic properties of tomato polygalacturonase isoenzymes.";
Eur. J. Biochem. 135:511-514(1983).
[12]
INTERACTION WITH GP1, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=6489331 [NCBI, ExPASy, EBI, Israel, Japan]
Pressey R.;
"Purification and characterization of tomato polygalacturonase converter.";
Eur. J. Biochem. 144:217-221(1984).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
DOI=10.1105/tpc.2.12.1239; PubMed=2152163 [NCBI, ExPASy, EBI, Israel, Japan]
Osteryoung K.W., Toenjes K., Hall B., Winkler V., Bennett A.B.;
"Analysis of tomato polygalacturonase expression in transgenic tobacco.";
Plant Cell 2:1239-1248(1990).
[14]
INTERACTION WITH GP1.
DOI=10.1007/BF00240897
Pogson B.J., Brady C.J.;
"Accumulation of the beta-subunit of polygalacturonase 1 in normal and mutant tomato fruit.";
Planta 191:71-78(1993).
[15]
FUNCTION, AND DEVELOPMENTAL STAGE.
DOI=10.1105/tpc.6.11.1623; PubMed=7827495 [NCBI, ExPASy, EBI, Israel, Japan]
Watson C.F., Zheng L., DellaPenna D.;
"Reduction of tomato polygalacturonase beta subunit expression affects pectin solubilization and degradation during fruit ripening.";
Plant Cell 6:1623-1634(1994).
[16]
DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION BY ETHYLENE.
PubMed=12232274 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng L., Watson C.F., DellaPenna D.;
"Differential expression of the two subunits of tomato polygalacturonase isoenzyme 1 in wild-type and in tomato fruit.";
Plant Physiol. 105:1189-1195(1994).
[17]
SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=12232422 [NCBI, ExPASy, EBI, Israel, Japan]
Moore T., Bennett A.B.;
"Tomato fruit polygalacturonase isozyme 1 -- characterization of the beta subunit and its state of assembly in vivo.";
Plant Physiol. 106:1461-1469(1994).
[18]
FUNCTION.
DOI=10.1023/A:1006086004262; PubMed=9747798 [NCBI, ExPASy, EBI, Israel, Japan]
Cooley M.B., Yoder J.I.;
"Insertional inactivation of the tomato polygalacturonase gene.";
Plant Mol. Biol. 38:521-530(1998).
[19]
ENZYME ACTIVITY.
DOI=10.1104/pp.117.4.1293; PubMed=9701584 [NCBI, ExPASy, EBI, Israel, Japan]
Chun J.-P., Huber D.J.;
"Polygalacturonase-mediated solubilization and depolymerization of pectic polymers in tomato fruit cell walls. Regulation By ph and ionic conditions.";
Plant Physiol. 117:1293-1299(1998).
[20]
BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1002/bit.10920; PubMed=15007842 [NCBI, ExPASy, EBI, Israel, Japan]
Verlent I., van Loey A., Smout C., Duvetter T., Hendrickx M.E.;
"Purified tomato polygalacturonase activity during thermal and high-pressure treatment.";
Biotechnol. Bioeng. 86:63-71(2004).
[21]
X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-368.
DOI=10.1107/S0907444903018092; PubMed=14646066 [NCBI, ExPASy, EBI, Israel, Japan]
Heffron S., Watkins S., Moeller R., Taban A.H., Butowt R., DellaPenna D., Jurnak F.;
"Resolving the space-group ambiguity of crystals of tomato fruit polygalacturonase.";
Acta Crystallogr. D 59:2088-2093(2003).
Comments
  • FUNCTION: Catalytic subunit of the polygalacturonase isozyme 1 and 2 (PG1 and PG2). Acts in concert with the pectinesterase, in the ripening process. Is involved in cell wall metabolism, specifically in polyuronide degradation. The depolymerization and solubilization of cell wall polyuronides mediated by PG2 during ripening seems to be limited by the beta subunit GP1, probably by recruiting PG2 to form PG1.
  • CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Absorption:   Abs(max)=276 nm;
    Note=The ratio of Abs(276)/Abs(260)=1.35. These values are for PG1;
    Kinetic parameters:   KM=38 µM for polygalacturonic acid (for PG2 at pH 4.6 and 35 degrees Celsius);
    KM=75 µM for polygalacturonic acid (for PG1 at pH 4.6 and 35 degrees Celsius);
    Vmax=58.8 µmol/min/mg enzyme (for PG2 at pH 4.6 and 35 degrees Celsius);
    Vmax=7 µmol/min/mg enzyme (for PG2 at pH 3.8 and 25 degrees Celsius);
    Vmax=27.7 µmol/min/mg enzyme (for PG1 at pH 4.6 and 35 degrees Celsius);
    Vmax=4 µmol/min/mg enzyme (for PG1 at pH 3.8 and 25 degrees Celsius);
    pH dependence:   Optimum pH is 4.4-4.8 at 35 degrees Celsius. PG1 is resistant to acidic but not to alkaline conditions, at which PG2 is released from the beta subunit;
    Temperature dependence:   Optimum temperature is 55-60 degrees Celsius at pH 4.4. PG1 is more thermostable than PG2;
  • SUBUNIT: Monomer PG2 (isoenzymes PG2A and PG2B). Also forms heterodimers called polygalacturonase 1 (PG1) with the beta subunit GP1.
  • SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. Secreted, cell wall. Note=Associated to the cell wall.
  • TISSUE SPECIFICITY: Expressed only in ripening fruits (at protein level).
  • DEVELOPMENTAL STAGE: PG1 appears when fruits start to be coloured. When fruits are orange, both PG2 and PG1 are present. In fully ripe fruit, mostly PG2 is expressed.
  • INDUCTION: By ethylene.
  • PTM: N-glycosylated. PG2B isozyme has a greater degree of glycosylation than PG2A.
  • BIOTECHNOLOGY: The effect of PG can be neutralized by introducing an antisense PG gene by genetic manipulation. The Flavr Savr tomato produced by Calgene (Monsanto) in such a manner has a longer shelf life due to delayed ripening.
  • MISCELLANEOUS: To ovoid liquid rheology of tomato juice, temperature and pressure can be increased to inactivate selectively PG2 during the process.
  • SIMILARITY: Belongs to the glycosyl hydrolase 28 family [view classification].
  • SIMILARITY: Contains 4 PbH1 repeats.
  • SEQUENCE CAUTION:
    • Sequence=CAD44521.1; Type=Frameshift; Positions=156, 161;
Copyright
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Cross-references
Sequence databases
EMBL
X04583; CAA28254.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05656; CAA29148.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14074; CAA32235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M37304; AAA34178.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A15981; CAA01256.1; -; Unassigned_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A24194; CAA01720.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20269; AAA34177.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07410; CAA30308.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ505947; CAD44521.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A25534; A25534.
UniGene Les.17635
3D structure databases
ModBase P05117.
Ontologies
GO
GO:0048046; Cellular component: apoplast (inferred from electronic annotation from UniProtKB-KW).
GO:0005618; Cellular component: cell wall (inferred from electronic annotation from UniProtKB-KW).
GO:0007047; Biological process: cell wall organization (inferred from electronic annotation from UniProtKB-KW).
GO:0009835; Biological process: ripening (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000743; Glyco_hydro_28.
IPR006626; PbH1.
IPR012334; Pectin_lyas_fold.
Graphical view of domain structure.
Gene3D G3DSA:2.160.20.10; Pectin_lyas_fold; 1.
Pfam PF00295; Glyco_hydro_28; 1.
Pfam graphical view of domain structure.
SMART SM00710; PbH1; 4.
SMART graphical view of domain structure.
PROSITE PS00502; POLYGALACTURONASE; 1.
BLOCKS P05117.
ProtoNet P05117.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoplast; Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing; Fruit ripening; Genetically modified food; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24      
PROPEP   25    71  47      PRO_0000024804
CHAIN   72   444  373     Polygalacturonase-2. PRO_0000024805
PROPEP   445   457  13      PRO_0000043095
REPEAT   228   255  28     PbH1 1. 
REPEAT   256   277  22     PbH1 2. 
REPEAT   309   330  22     PbH1 3. 
REPEAT   338   359  22     PbH1 4. 
ACT_SITE   270   270        Proton donor (By similarity). 
ACT_SITE   293   293        By similarity. 
CARBOHYD   189   189        N-linked (GlcNAc...) (Potential). 
CARBOHYD   240   240        N-linked (GlcNAc...) (Potential). 
CARBOHYD   286   286        N-linked (GlcNAc...) (Potential). 
CARBOHYD   311   311        N-linked (GlcNAc...) (Potential). 
CONFLICT   96    96        E -> Q (in Ref. 1; AA sequence). 
CONFLICT   136   136        V -> E (in Ref. 8; CAD44521). 
CONFLICT   169   169        G -> E (in Ref. 8; CAD44521). 
Sequence information
Length: 457 AA [This is the length of the unprocessed precursor] Molecular weight: 50052 Da [This is the MW of the unprocessed precursor] CRC64: 449E4DC36919B074 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVIQRNSILL LIIIFASSIS TCRSNVIDDN LFKQVYDNIL EQEFAHDFQA YLSYLSKNIE 

        70         80         90        100        110        120 
SNNNIDKVDK NGIKVINVLS FGAKGDGKTY DNIAFEQAWN EACSSRTPVQ FVVPKNKNYL 

       130        140        150        160        170        180 
LKQITFSGPC RSSISVKIFG SLEASSKISD YKDRRLWIAF DSVQNLVVGG GGTINGNGQV 

       190        200        210        220        230        240 
WWPSSCKINK SLPCRDAPTA LTFWNCKNLK VNNLKSKNAQ QIHIKFESCT NVVASNLMIN 

       250        260        270        280        290        300 
ASAKSPNTDG VHVSNTQYIQ ISDTIIGTGD DCISIVSGSQ NVQATNITCG PGHGISIGSL 

       310        320        330        340        350        360 
GSGNSEAYVS NVTVNEAKII GAENGVRIKT WQGGSGQASN IKFLNVEMQD VKYPIIIDQN 

       370        380        390        400        410        420 
YCDRVEPCIQ QFSAVQVKNV VYENIKGTSA TKVAIKFDCS TNFPCEGIIM ENINLVGESG 

       430        440        450 
KPSEATCKNV HFNNAEHVTP HCTSLEISED EALLYNY 

P05117 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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