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InterPro: IPR013812 Glycoside hydrolase, family 2/20, immunoglobulin-like beta-sandwich domain

Protein matchesHelp
UniProtKB
Matches:
1863 proteins
AccessionHelp IPR013812 Glyco_hydro_2/20_Ig-like
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004867 Glycoside hydrolase, family 20, C-terminal
IPR006102 Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 2 GH2 comprises enzymes with several known activities: beta-galactosidase (EC:3.2.1.23); beta-mannosidase (EC:3.2.1.25); beta-glucuronidase (EC:3.2.1.31).

Glycoside hydrolase family 20 GH20 consists of enzymes such as chitobiases and beta-hexosaminidases (EC:3.2.1.52), in which this immunoglobulin-like domain occurs at the C terminus [5, 6].

This entry describes the immunoglobulin-like beta-sandwich domain that consists of seven beta-strands in two sheets with a Greek-key topology, although some members may have extra strands. This fold is found in domains of glycoside hydrolase families 2 and 20. The function of this domain is unknown.

Structural linksHelp
CATH: 2.60.40.320
Database linksHelp
Enzyme: EC:3.2.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR013812 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O18835 Beta-glucuronidase

P00722 Beta-galactosidase

P08236 Beta-glucuronidase

P12265 Beta-glucuronidase

Q75W54 Mannosylglycoprotein endo-beta-mannosidase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR004199 Glycoside hydrolase, family 42, domain 5
IPR013812 Glycoside hydrolase, family 2/20, immunoglobulin-like beta-sandwich domain
IPR011013 Glycoside hydrolase-type carbohydrate-binding
IPR006101 Glycoside hydrolase, family 2
IPR008979 Galactose-binding domain-like
IPR006104 Glycoside hydrolase family 2, carbohydrate-binding
IPR017853 Glycoside hydrolase, catalytic core
IPR006102 Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich
IPR006103 Glycoside hydrolase family 2, TIM barrel
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. 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
2. 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
3. Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
4. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
5. Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE.
Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease.
Nat. Struct. Biol. 3 638-48 1996 [PubMed: 8673609]
http://dx.doi.org/10.1038/nsb0796-638
6. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW.
Three-dimensional structure of beta-galactosidase from E. coli.
Nature 369 761-6 1994 [PubMed: 8008071]
http://dx.doi.org/10.1038/369761a0

Additional ReadingHelp
Juers DH, Hakda S, Matthews BW, Huber RE.
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase.
Biochemistry 42 2003 13505-11 [PubMed: 14621996]
http://dx.doi.org/10.1021/bi035506j
Juers DH, Matthews BW.
Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions.
J. Mol. Biol. 311 2001 851-62 [PubMed: 11518535]
http://dx.doi.org/10.1006/jmbi.2001.4891
Prag G, Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Oppenheim AB.
Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540.
J. Mol. Biol. 300 2000 611-7 [PubMed: 10884356]
http://dx.doi.org/10.1006/jmbi.2000.3906
Skalova T, Dohnalek J, Spiwok V, Lipovova P, Vondrackova E, Petrokova H, Duskova J, Strnad H, Kralova B, Hasek J.
Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution.
J. Mol. Biol. 353 2005 282-94 [PubMed: 16171818]
http://dx.doi.org/10.1016/j.jmb.2005.08.028
Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW.
A structural view of the action of Escherichia coli (lacZ) beta-galactosidase.
Biochemistry 40 2001 14781-94 [PubMed: 11732897]
http://dx.doi.org/10.1021/bi011727i
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InterPro 23.1