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PROSITE documentation PDOC00415

Polygalacturonase active site

Description:

Polygalacturonase (EC 3.2.1.15) (PG) (pectinase) [1,2] catalyzes the random hydrolysis of 1,4-α-D-galactosiduronic linkages in pectate and other galacturonans. In fruit, polygalacturonase plays an important role in cell wall metabolism during ripening. In plant bacterial pathogens such as Erwinia carotovora or Pseudomonas solanacearum and fungal pathogens such as Aspergillus niger, polygalacturonase is involved in maceration and soft-rotting of plant tissue.

Exo-poly-α-D-galacturonosidase (EC 3.2.1.82) (exoPG) [3] hydrolyzes peptic acid from the non-reducing end, releasing digalacturonate.

Prokaryotic, eukaryotic PG and exoPG share a few regions of sequence similarity. We selected the best conserved of these regions, which is centered on a conserved histidine most probably involved in the catalytic mechanism [4].

Note:

These proteins belong to family 28 in the classification of glycosyl hydrolases [5,E1].

Last update:

May 2004 / Text revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

POLYGALACTURONASE, PS00502; Polygalacturonase active site  (PATTERN)
Consensus pattern: [GSDENKRH]-x(2)-[VMFC]-x(2)-[GS]-H-G-[LIVMAG]-x(1,2)-[LIVM]-G-S
H may be the active site residue
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00502
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00502
• Scan Swiss-Prot/TrEMBL entries against PS00502
• view ligand binding statistics
Matching PDB structures: 1BHE 1CZF 1HG8 1IA5 ... [ALL]

References:

1 AuthorsRuttowski E., Labitzke R., Khanh N.Q., Loeffler F., Gottschalk M., Jany K.-D.
SourceBiochim. Biophys. Acta 1087:104-106(1990).
2 AuthorsHuang J.H., Schell M.A.
TitleDNA sequence analysis of pglA and mechanism of export of its polygalacturonase product from Pseudomonas solanacearum.
SourceJ. Bacteriol. 172:3879-3887(1990).
PubMed ID2193922
3 AuthorsHe S.Y., Collmer A.
TitleMolecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16.
SourceJ. Bacteriol. 172:4988-4995(1990).
PubMed ID2168372
4 AuthorsBussink H.J.D., Buxton F.P., Visser J.
TitleExpression and sequence comparison of the Aspergillus niger and Aspergillus tubigensis genes encoding polygalacturonase II.
SourceCurr. Genet. 19:467-474(1991).
PubMed ID1878999
5 AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104
E1
Sourcehttp://www.expasy.org/cgi-bin/lists?glycosid.txt

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