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Polygalacturonase-2 (PG) (EC 3.2.1.15) (PG-2A) (PG-2B) (Pectinase)

 PGLR_SOLLC              Reviewed;         457 AA.
P05117; P94004; Q70Y18; Q7DM56;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
07-JUN-2017, entry version 125.
RecName: Full=Polygalacturonase-2;
Short=PG;
EC=3.2.1.15;
AltName: Full=PG-2A;
AltName: Full=PG-2B;
AltName: Full=Pectinase;
Flags: Precursor;
Name=PG2; Synonyms=PG, PG2A, PG2B;
Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
Solaneae; Solanum; Lycopersicon.
NCBI_TaxID=4081;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 72-96.
STRAIN=cv. Ailsa Craig;
PubMed=3786135; DOI=10.1093/nar/14.21.8595;
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;
AGRICOLA=IND92000010; DOI=10.1007/BF00017465;
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; DOI=10.1104/pp.86.4.1057;
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.
PubMed=3405769; DOI=10.1093/nar/16.14.7191;
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; DOI=10.1111/j.1432-1033.1980.tb04993.x;
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;
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; DOI=10.1111/j.1432-1033.1983.tb07681.x;
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; DOI=10.1111/j.1432-1033.1984.tb08452.x;
Pressey R.;
"Purification and characterization of tomato polygalacturonase
converter.";
Eur. J. Biochem. 144:217-221(1984).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=2152163; DOI=10.1105/tpc.2.12.1239;
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.
PubMed=7827495; DOI=10.1105/tpc.6.11.1623;
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; DOI=10.1104/pp.105.4.1189;
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; DOI=10.1104/pp.106.4.1461;
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.
PubMed=9747798; DOI=10.1023/A:1006086004262;
Cooley M.B., Yoder J.I.;
"Insertional inactivation of the tomato polygalacturonase gene.";
Plant Mol. Biol. 38:521-530(1998).
[19]
ENZYME ACTIVITY.
PubMed=9701584; DOI=10.1104/pp.117.4.1293;
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.
PubMed=15007842; DOI=10.1002/bit.10920;
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.
PubMed=14646066; DOI=10.1107/S0907444903018092;
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).
-!- 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. {ECO:0000269|PubMed:2152163,
ECO:0000269|PubMed:7827495, ECO:0000269|PubMed:9747798}.
-!- CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-alpha-D-
galactosiduronic linkages in pectate and other galacturonans.
{ECO:0000269|PubMed:9701584}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=276 nm {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
Note=The ratio of Abs(276)/Abs(260)=1.35. These values are for
PG1.;
Kinetic parameters:
KM=38 uM for polygalacturonic acid (for PG2 at pH 4.6 and 35
degrees Celsius) {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
KM=75 uM for polygalacturonic acid (for PG1 at pH 4.6 and 35
degrees Celsius) {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
Vmax=58.8 umol/min/mg enzyme (for PG2 at pH 4.6 and 35 degrees
Celsius) {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
Vmax=7 umol/min/mg enzyme (for PG2 at pH 3.8 and 25 degrees
Celsius) {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
Vmax=27.7 umol/min/mg enzyme (for PG1 at pH 4.6 and 35 degrees
Celsius) {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
Vmax=4 umol/min/mg enzyme (for PG1 at pH 3.8 and 25 degrees
Celsius) {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
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. {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
Temperature dependence:
Optimum temperature is 55-60 degrees Celsius at pH 4.4. PG1 is
more thermostable than PG2. {ECO:0000269|PubMed:15007842,
ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647,
ECO:0000269|PubMed:7449759};
-!- SUBUNIT: Monomer PG2 (isoenzymes PG2A and PG2B). Also forms
heterodimers called polygalacturonase 1 (PG1) with the beta
subunit GP1. {ECO:0000269|PubMed:12232422,
ECO:0000269|PubMed:7227374, ECO:0000269|PubMed:7449759}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
{ECO:0000269|PubMed:2152163}. Secreted, cell wall
{ECO:0000269|PubMed:2152163}. Note=Associated to the cell wall.
-!- TISSUE SPECIFICITY: Expressed only in ripening fruits (at protein
level). {ECO:0000269|PubMed:12232274, ECO:0000269|PubMed:12232422,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
-!- 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. {ECO:0000269|PubMed:12232274,
ECO:0000269|PubMed:7449759, ECO:0000269|PubMed:7827495}.
-!- INDUCTION: By ethylene. {ECO:0000269|PubMed:12232274}.
-!- PTM: N-glycosylated. PG2B isozyme has a greater degree of
glycosylation than PG2A. {ECO:0000269|PubMed:16666031,
ECO:0000269|PubMed:2152163, ECO:0000269|PubMed:6617647}.
-!- 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 avoid 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.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD44521.1; Type=Frameshift; Positions=156, 161; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X04583; CAA28254.1; -; mRNA.
EMBL; X05656; CAA29148.1; -; mRNA.
EMBL; X14074; CAA32235.1; -; Genomic_DNA.
EMBL; M37304; AAA34178.1; -; Genomic_DNA.
EMBL; A15981; CAA01256.1; -; Unassigned_RNA.
EMBL; A24194; CAA01720.1; -; Unassigned_DNA.
EMBL; M20269; AAA34177.1; -; mRNA.
EMBL; X07410; CAA30308.1; -; Genomic_DNA.
EMBL; AJ505947; CAD44521.1; ALT_FRAME; mRNA.
PIR; A25534; A25534.
RefSeq; NP_001234021.1; NM_001247092.2.
UniGene; Les.17635; -.
UniGene; Les.4463; -.
ProteinModelPortal; P05117; -.
SMR; P05117; -.
STRING; 4081.Solyc10g080210.1.1; -.
Allergome; 6157; Sola l PG.
CAZy; GH28; Glycoside Hydrolase Family 28.
PaxDb; P05117; -.
PRIDE; P05117; -.
EnsemblPlants; Solyc10g080210.1.1; Solyc10g080210.1.1; Solyc10g080210.1.
GeneID; 544051; -.
Gramene; Solyc10g080210.1.1; Solyc10g080210.1.1; Solyc10g080210.1.
KEGG; sly:544051; -.
eggNOG; ENOG410IF8F; Eukaryota.
eggNOG; COG5434; LUCA.
InParanoid; P05117; -.
KO; K01213; -.
OMA; QSCYGED; -.
OrthoDB; EOG09360ADQ; -.
Proteomes; UP000004994; Chromosome 10.
GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR000743; Glyco_hydro_28.
InterPro; IPR006626; PbH1.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
Pfam; PF00295; Glyco_hydro_28; 1.
SMART; SM00710; PbH1; 4.
SUPFAM; SSF51126; SSF51126; 1.
PROSITE; PS00502; POLYGALACTURONASE; 1.
1: Evidence at protein level;
Apoplast; Cell wall; Cell wall biogenesis/degradation;
Complete proteome; Direct protein sequencing; Fruit ripening;
Genetically modified food; Glycoprotein; Glycosidase; Hydrolase;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:16666031}.
PROPEP 25 71
/FTId=PRO_0000024804.
CHAIN 72 444 Polygalacturonase-2.
/FTId=PRO_0000024805.
PROPEP 445 457 {ECO:0000269|PubMed:16666031}.
/FTId=PRO_0000043095.
REPEAT 228 255 PbH1 1.
REPEAT 256 277 PbH1 2.
REPEAT 309 330 PbH1 3.
REPEAT 338 359 PbH1 4.
ACT_SITE 270 270 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10052}.
ACT_SITE 293 293 {ECO:0000255|PROSITE-ProRule:PRU10052}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 96 96 E -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 136 136 V -> E (in Ref. 8; CAD44521).
{ECO:0000305}.
CONFLICT 169 169 G -> E (in Ref. 8; CAD44521).
{ECO:0000305}.
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


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