Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05117

- PGLR_SOLLC

UniProt

P05117 - PGLR_SOLLC

Protein

Polygalacturonase-2

Gene

PG2

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 PG1.3 Publications

    Catalytic activityi

    Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.1 Publication

    Absorptioni

    Abs(max)=276 nm4 Publications

    The ratio of Abs(276)/Abs(260)=1.35. These values are for PG1.

    Kineticsi

    1. KM=38 µM for polygalacturonic acid (for PG2 at pH 4.6 and 35 degrees Celsius)4 Publications
    2. KM=75 µM for polygalacturonic acid (for PG1 at pH 4.6 and 35 degrees Celsius)4 Publications

    Vmax=58.8 µmol/min/mg enzyme (for PG2 at pH 4.6 and 35 degrees Celsius)4 Publications

    Vmax=7 µmol/min/mg enzyme (for PG2 at pH 3.8 and 25 degrees Celsius)4 Publications

    Vmax=27.7 µmol/min/mg enzyme (for PG1 at pH 4.6 and 35 degrees Celsius)4 Publications

    Vmax=4 µmol/min/mg enzyme (for PG1 at pH 3.8 and 25 degrees Celsius)4 Publications

    pH dependencei

    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.4 Publications

    Temperature dependencei

    Optimum temperature is 55-60 degrees Celsius at pH 4.4. PG1 is more thermostable than PG2.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei270 – 2701Proton donorPROSITE-ProRule annotation
    Active sitei293 – 2931PROSITE-ProRule annotation

    GO - Molecular functioni

    1. polygalacturonase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. fruit ripening Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation, Fruit ripening

    Protein family/group databases

    CAZyiGH28. Glycoside Hydrolase Family 28.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polygalacturonase-2 (EC:3.2.1.15)
    Short name:
    PG
    Alternative name(s):
    PG-2A
    PG-2B
    Pectinase
    Gene namesi
    Name:PG2
    Synonyms:PG, PG2A, PG2B
    OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
    Taxonomic identifieri4081 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
    ProteomesiUP000004994: Chromosome 10

    Subcellular locationi

    Secretedextracellular spaceapoplast 1 Publication. Secretedcell wall 1 Publication
    Note: Associated to the cell wall.

    GO - Cellular componenti

    1. apoplast Source: UniProtKB-SubCell
    2. cell wall Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apoplast, Cell wall, Secreted

    Pathology & Biotechi

    Biotechnological usei

    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.

    Protein family/group databases

    Allergomei6157. Sola l PG.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Propeptidei25 – 7147PRO_0000024804Add
    BLAST
    Chaini72 – 444373Polygalacturonase-2PRO_0000024805Add
    BLAST
    Propeptidei445 – 457131 PublicationPRO_0000043095Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. PG2B isozyme has a greater degree of glycosylation than PG2A.3 Publications

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed only in ripening fruits (at protein level).4 Publications

    Developmental stagei

    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.3 Publications

    Inductioni

    By ethylene.1 Publication

    Interactioni

    Subunit structurei

    Monomer PG2 (isoenzymes PG2A and PG2B). Also forms heterodimers called polygalacturonase 1 (PG1) with the beta subunit GP1.3 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliP05117.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati228 – 25528PbH1 1Add
    BLAST
    Repeati256 – 27722PbH1 2Add
    BLAST
    Repeati309 – 33022PbH1 3Add
    BLAST
    Repeati338 – 35922PbH1 4Add
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 28 family.Curated
    Contains 4 PbH1 repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    OMAiKANGNDD.

    Family and domain databases

    Gene3Di2.160.20.10. 1 hit.
    InterProiIPR000743. Glyco_hydro_28.
    IPR006626. PbH1.
    IPR012334. Pectin_lyas_fold.
    IPR011050. Pectin_lyase_fold/virulence.
    [Graphical view]
    PfamiPF00295. Glyco_hydro_28. 1 hit.
    [Graphical view]
    SMARTiSM00710. PbH1. 4 hits.
    [Graphical view]
    SUPFAMiSSF51126. SSF51126. 1 hit.
    PROSITEiPS00502. POLYGALACTURONASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05117-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVIQRNSILL LIIIFASSIS TCRSNVIDDN LFKQVYDNIL EQEFAHDFQA    50
    YLSYLSKNIE SNNNIDKVDK NGIKVINVLS FGAKGDGKTY DNIAFEQAWN 100
    EACSSRTPVQ FVVPKNKNYL LKQITFSGPC RSSISVKIFG SLEASSKISD 150
    YKDRRLWIAF DSVQNLVVGG GGTINGNGQV WWPSSCKINK SLPCRDAPTA 200
    LTFWNCKNLK VNNLKSKNAQ QIHIKFESCT NVVASNLMIN ASAKSPNTDG 250
    VHVSNTQYIQ ISDTIIGTGD DCISIVSGSQ NVQATNITCG PGHGISIGSL 300
    GSGNSEAYVS NVTVNEAKII GAENGVRIKT WQGGSGQASN IKFLNVEMQD 350
    VKYPIIIDQN YCDRVEPCIQ QFSAVQVKNV VYENIKGTSA TKVAIKFDCS 400
    TNFPCEGIIM ENINLVGESG KPSEATCKNV HFNNAEHVTP HCTSLEISED 450
    EALLYNY 457
    Length:457
    Mass (Da):50,052
    Last modified:August 13, 1987 - v1
    Checksum:i449E4DC36919B074
    GO

    Sequence cautioni

    The sequence CAD44521.1 differs from that shown. Reason: Frameshift at positions 156 and 161.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961E → Q AA sequence (PubMed:3786135)Curated
    Sequence conflicti136 – 1361V → E in CAD44521. 1 PublicationCurated
    Sequence conflicti169 – 1691G → E in CAD44521. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04583 mRNA. Translation: CAA28254.1.
    X05656 mRNA. Translation: CAA29148.1.
    X14074 Genomic DNA. Translation: CAA32235.1.
    M37304 Genomic DNA. Translation: AAA34178.1.
    A15981 Unassigned RNA. Translation: CAA01256.1.
    A24194 Unassigned DNA. Translation: CAA01720.1.
    M20269 mRNA. Translation: AAA34177.1.
    X07410 Genomic DNA. Translation: CAA30308.1.
    AJ505947 mRNA. Translation: CAD44521.1. Frameshift.
    PIRiA25534.
    RefSeqiNP_001234021.1. NM_001247092.2.
    UniGeneiLes.17635.
    Les.4463.

    Genome annotation databases

    EnsemblPlantsiSolyc10g080210.1.1; Solyc10g080210.1.1; Solyc10g080210.1.
    GeneIDi544051.
    KEGGisly:544051.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04583 mRNA. Translation: CAA28254.1 .
    X05656 mRNA. Translation: CAA29148.1 .
    X14074 Genomic DNA. Translation: CAA32235.1 .
    M37304 Genomic DNA. Translation: AAA34178.1 .
    A15981 Unassigned RNA. Translation: CAA01256.1 .
    A24194 Unassigned DNA. Translation: CAA01720.1 .
    M20269 mRNA. Translation: AAA34177.1 .
    X07410 Genomic DNA. Translation: CAA30308.1 .
    AJ505947 mRNA. Translation: CAD44521.1 . Frameshift.
    PIRi A25534.
    RefSeqi NP_001234021.1. NM_001247092.2.
    UniGenei Les.17635.
    Les.4463.

    3D structure databases

    ProteinModelPortali P05117.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 6157. Sola l PG.
    CAZyi GH28. Glycoside Hydrolase Family 28.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi Solyc10g080210.1.1 ; Solyc10g080210.1.1 ; Solyc10g080210.1 .
    GeneIDi 544051.
    KEGGi sly:544051.

    Phylogenomic databases

    OMAi KANGNDD.

    Family and domain databases

    Gene3Di 2.160.20.10. 1 hit.
    InterProi IPR000743. Glyco_hydro_28.
    IPR006626. PbH1.
    IPR012334. Pectin_lyas_fold.
    IPR011050. Pectin_lyase_fold/virulence.
    [Graphical view ]
    Pfami PF00295. Glyco_hydro_28. 1 hit.
    [Graphical view ]
    SMARTi SM00710. PbH1. 4 hits.
    [Graphical view ]
    SUPFAMi SSF51126. SSF51126. 1 hit.
    PROSITEi PS00502. POLYGALACTURONASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing and identification of a cDNA clone for tomato polygalacturonase."
      Grierson D., Tucker G.A., Keen J., Ray J., Bird C.R., Schuch W.
      Nucleic Acids Res. 14:8595-8603(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-96.
      Strain: cv. Ailsa Craig.
    2. "Molecular characterization of tomato fruit polygalacturonase."
      Sheehy R.E., Pearson J., Brady C.J., Hiatt W.R.
      Mol. Gen. Genet. 208:30-36(1987)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
    3. Hiatt W.R.
      Submitted (OCT-1987) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "The tomato polygalacturonase gene and ripening-specific expression in transgenic plants."
      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.
      Plant Mol. Biol. 11:651-662(1988)
      [AGRICOLA] [Europe PMC]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: cv. Ailsa Craig.
    5. "Anti-sense regulation of plant gene expression."
      Bridges I.G., Schuch W.W., Grierson D.
      Patent number EP0271988, 22-JUN-1988
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: cv. Ailsa Craig.
    6. "In vitro synthesis and processing of tomato fruit polygalacturonase."
      DellaPenna D., Bennett A.B.
      Plant Physiol. 86:1057-1063(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-115, PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN SEQUENCE OF 72-92, GLYCOSYLATION.
    7. "The nucleotide sequence of the 5' flanking region of a tomato polygalacturonase gene."
      Rose R.E., Houck C.M., Monson E.K., DeJesus C.E., Sheehy R.E., Hiatt W.R.
      Nucleic Acids Res. 16:7191-7191(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
    8. "Isolation, cloning and characterization of polygalacturonase gene from fruit tissue of Lycopersicum esculentum cv. Arka vikas."
      Saiprasad G.V.S.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 96-294.
      Strain: cv. Arka vikas.
      Tissue: Fruit.
    9. "Changes in polygalacturonase isoenzymes during the 'ripening' of normal and mutant tomato fruit."
      Tucker G.A., Robertson N.G., Grierson D.
      Eur. J. Biochem. 112:119-124(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DEVELOPMENTAL STAGE.
    10. "The conversion of tomato-fruit polygalacturonase isoenzyme 2 into isoenzyme 1 in vitro."
      Tucker G.A., Robertson N.G., Grierson D.
      Eur. J. Biochem. 115:87-90(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Carbohydrate composition and electrophoretic properties of tomato polygalacturonase isoenzymes."
      Moshrefi M., Luh B.S.
      Eur. J. Biochem. 135:511-514(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION.
    12. "Purification and characterization of tomato polygalacturonase converter."
      Pressey R.
      Eur. J. Biochem. 144:217-221(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GP1, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Analysis of tomato polygalacturonase expression in transgenic tobacco."
      Osteryoung K.W., Toenjes K., Hall B., Winkler V., Bennett A.B.
      Plant Cell 2:1239-1248(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION.
    14. "Accumulation of the beta-subunit of polygalacturonase 1 in normal and mutant tomato fruit."
      Pogson B.J., Brady C.J.
      Planta 191:71-78(1993)
      Cited for: INTERACTION WITH GP1.
    15. "Reduction of tomato polygalacturonase beta subunit expression affects pectin solubilization and degradation during fruit ripening."
      Watson C.F., Zheng L., DellaPenna D.
      Plant Cell 6:1623-1634(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    16. "Differential expression of the two subunits of tomato polygalacturonase isoenzyme 1 in wild-type and in tomato fruit."
      Zheng L., Watson C.F., DellaPenna D.
      Plant Physiol. 105:1189-1195(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INDUCTION BY ETHYLENE.
    17. "Tomato fruit polygalacturonase isozyme 1 -- characterization of the beta subunit and its state of assembly in vivo."
      Moore T., Bennett A.B.
      Plant Physiol. 106:1461-1469(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, TISSUE SPECIFICITY.
    18. "Insertional inactivation of the tomato polygalacturonase gene."
      Cooley M.B., Yoder J.I.
      Plant Mol. Biol. 38:521-530(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Polygalacturonase-mediated solubilization and depolymerization of pectic polymers in tomato fruit cell walls. Regulation By ph and ionic conditions."
      Chun J.-P., Huber D.J.
      Plant Physiol. 117:1293-1299(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY.
    20. "Purified tomato polygalacturonase activity during thermal and high-pressure treatment."
      Verlent I., van Loey A., Smout C., Duvetter T., Hendrickx M.E.
      Biotechnol. Bioeng. 86:63-71(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    21. "Resolving the space-group ambiguity of crystals of tomato fruit polygalacturonase."
      Heffron S., Watkins S., Moeller R., Taban A.H., Butowt R., DellaPenna D., Jurnak F.
      Acta Crystallogr. D 59:2088-2093(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-368.

    Entry informationi

    Entry nameiPGLR_SOLLC
    AccessioniPrimary (citable) accession number: P05117
    Secondary accession number(s): P94004, Q70Y18, Q7DM56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    To avoid liquid rheology of tomato juice, temperature and pressure can be increased to inactivate selectively PG2 during the process.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Genetically modified food, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3