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InterPro: IPR000743 Glycoside hydrolase, family 28
Protein matches
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UniProtKB Matches: 1891 proteins |
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Accession
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IPR000743 Glyco_hydro_28 |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR006626 Parallel beta-helix repeat
IPR012334 Pectin lyase fold
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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GO:0004650 polygalacturonase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
Glycoside hydrolase family 28 GH28 comprises enzymes with several known activities; polygalacturonase (EC:3.2.1.15); exo-polygalacturonase (EC:3.2.1.67); exo-polygalacturonase (EC:3.2.1.82); rhamnogalacturonase (EC not defined).
Polygalacturonase (PG) (pectinase) [5, 6] catalyses the random hydrolysis of 1,4-alpha-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 Ralstonia solanacearum (Pseudomonas solanacearum) and fungal pathogens such as Aspergillus niger, polygalacturonase is involved in maceration and soft-rotting of plant tissue. Exo-poly-alpha-D-galacturonosidase (EC:3.2.1.82) (exoPG) [7] hydrolyses peptic acid from the non-reducing end, releasing digalacturonate. PG and exoPG share a few regions of sequence similarity, and belong to family 28 of the glycosyl hydrolases.
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Structural links
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Database links
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Pfam Clan: CL0268.3
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Publications
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1.
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Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995
[PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
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2.
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Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995
[PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
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3.
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Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
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4.
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Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
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5.
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Ruttkowski E, Labitzke R, Khanh NQ, Loffler F, Gottschalk M, Jany KD.
Cloning and DNA sequence analysis of a polygalacturonase cDNA from Aspergillus niger RH5344.
Biochim. Biophys. Acta 1087 104-6 1990
[PubMed: 2400785]
http://dx.doi.org/10.1016/0167-4781(90)90130-T
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6.
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Huang JH, Schell MA.
DNA sequence analysis of pglA and mechanism of export of its polygalacturonase product from Pseudomonas solanacearum.
J. Bacteriol. 172 3879-87 1990
[PubMed: 2193922]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2193922
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7.
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He SY, Collmer A.
Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16.
J. Bacteriol. 172 4988-95 1990
[PubMed: 2168372]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2168372
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Additional Reading
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Federici L, Caprari C, Mattei B, Savino C, Di Matteo A, De Lorenzo G, Cervone F, Tsernoglou D.
Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein).
Proc. Natl. Acad. Sci. U.S.A. 98 2001 13425-30
[PubMed: 11687632]
http://dx.doi.org/10.1073/pnas.231473698
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Henrissat B.
A classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 280 ( Pt 2) 1991 309-16
[PubMed: 1747104]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
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Petersen TN, Kauppinen S, Larsen S.
The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix.
Structure 5 1997 533-44
[PubMed: 9115442]
http://dx.doi.org/10.1016/S0969-2126(97)00209-8
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Bussink HJ, Buxton FP, Visser J.
Expression and sequence comparison of the Aspergillus niger and Aspergillus tubigensis genes encoding polygalacturonase II.
Curr. Genet. 19 1991 467-74
[PubMed: 1878999]
http://dx.doi.org/10.1007/BF00312738
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van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW.
Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger.
FEBS Lett. 554 2003 462-6
[PubMed: 14623112]
http://dx.doi.org/10.1016/S0014-5793(03)01221-3
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Bonivento D, Pontiggia D, Matteo AD, Fernandez-Recio J, Salvi G, Tsernoglou D, Cervone F, Lorenzo GD, Federici L.
Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonase-inhibiting proteins.
Proteins 70 2008 294-9
[PubMed: 17876815]
http://dx.doi.org/10.1002/prot.21610
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Cho SW, Lee S, Shin W.
The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex.
J. Mol. Biol. 311 2001 863-78
[PubMed: 11518536]
http://dx.doi.org/10.1006/jmbi.2001.4919
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Shimizu T, Nakatsu T, Miyairi K, Okuno T, Kato H.
Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution.
Biochemistry 41 2002 6651-9
[PubMed: 12022868]
http://dx.doi.org/10.1021/bi025541a
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InterPro 23.1
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