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InterPro: IPR006101 Glycoside hydrolase, family 2
Protein matches
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UniProtKB Matches: 1578 proteins |
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Accession
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IPR006101 Glyco_hydro_2 |
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Secondary
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IPR001649
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Type
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Domain |
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Signatures
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InterPro Relationships
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Contains
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IPR006102 Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich
IPR006103 Glycoside hydrolase family 2, TIM barrel
IPR006104 Glycoside hydrolase family 2, carbohydrate-binding
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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:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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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 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).
These enzymes contain a conserved glutamic acid residue which has been shown [5], in Escherichia coli lacZ (P00722), to be the general acid/base catalyst in the active site of the enzyme.
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Structural links
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Database links
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Example proteins
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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 |
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| IPR013781 |
Glycoside hydrolase, subgroup, catalytic core |
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| IPR004199 |
Glycoside hydrolase, family 42, domain 5 |
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| IPR013812 |
Glycoside hydrolase, family 2/20, immunoglobulin-like beta-sandwich domain |
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| IPR011013 |
Glycoside hydrolase-type carbohydrate-binding |
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| IPR006101 |
Glycoside hydrolase, family 2 |
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| IPR008979 |
Galactose-binding domain-like |
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| IPR006104 |
Glycoside hydrolase family 2, carbohydrate-binding |
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| IPR017853 |
Glycoside hydrolase, catalytic core |
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| IPR006102 |
Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich |
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| IPR006103 |
Glycoside hydrolase family 2, TIM barrel |
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PDB Chain |
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ModBase |
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CATH Domain |
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SWISS-MODEL |
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SCOP Domain |
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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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Gebler JC, Aebersold R, Withers SG.
Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli.
J. Biol. Chem. 267 11126-30 1992
[PubMed: 1350782]
http://intl.jbc.org/cgi/reprint/267/16/11126.pdf
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Additional Reading
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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
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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
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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
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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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Schroeder CJ, Robert C, Lenzen G, McKay LL, Mercenier A.
Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus beta-galactosidase sequences.
J. Gen. Microbiol. 137 1991 369-80
[PubMed: 1901904]
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Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW.
High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation.
Protein Sci. 9 2000 1685-99
[PubMed: 11045615]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=11045615&action=stream&blobtype=pdf
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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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InterPro 23.1
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