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InterPro: IPR013781 Glycoside hydrolase, subgroup, catalytic core
Protein matches
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UniProtKB Matches: 36454 proteins |
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Accession
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IPR013781 Glyco_hydro_sg_catalytic |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR017853 Glycoside hydrolase, catalytic core
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Children
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IPR000933 Glycoside hydrolase, family 29
IPR001223 Glycoside hydrolase, family 18, catalytic domain
IPR001547 Glycoside hydrolase, family 5
IPR002053 Glycoside hydrolase, family 25
IPR006047 Glycosyl hydrolase, family 13, catalytic domain
IPR006103 Glycoside hydrolase family 2, TIM barrel
IPR011100 Glycosyl hydrolase 67 middle
IPR015883 Glycoside hydrolase, family 20, catalytic core
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Found in
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IPR000125 Glycoside hydrolase, family 14A, bacterial
IPR000490 Glycoside hydrolase, family 17
IPR000514 Glycoside hydrolase, family 39
IPR001000 Glycoside hydrolase, family 10
IPR001139 Glycoside hydrolase, family 30
IPR001286 Glycoside hydrolase, family 59
IPR001360 Glycoside hydrolase, family 1
IPR001371 Glycoside hydrolase, family 14B, plant
IPR001554 Glycoside hydrolase, family 14
IPR001944 Glycoside hydrolase, family 35
IPR003318 Glycoside hydrolase, family 70, catalytic core
IPR003385 Glycoside hydrolase, family 77
IPR003476 Glycoside hydrolase, family 42
IPR003790 Protein of unknown function DUF187
IPR004886 Glycolipid anchored surface protein GAS1
IPR005928 6-phospho-beta-galactosidase
IPR006407 1,4-alpha-glucan branching enzyme, core region
IPR006421 Glycogen debranching enzyme
IPR011683 Glycosyl hydrolase 53
IPR012665 Trehalose synthase
IPR013529 Glycoside hydrolase, family 42, N-terminal
IPR016714 Mannan endo-1,4-beta-mannosidase
IPR017736 Glycoside hydrolase, family 1, beta-glucosidase
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Contains
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IPR001579 Glycoside hydrolase, chitinase active site
IPR006589 Glycosyl hydrolase, family 13, subfamily, catalytic domain
IPR008270 Glycoside hydrolase, family 25, active site
IPR018087 Glycoside hydrolase, family 5, conserved site
IPR018120 Glycoside hydrolase, family 1, active site
IPR018238 Glycoside hydrolase, family 14, conserved site
IPR018526 Glycoside hydrolase, family 29, conserved site
IPR019801 Glycoside hydrolase, family 35, conserved site
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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:0003824 catalytic activity
GO:0043169 cation binding
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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.
This entry represents the catalytic TIM beta/alpha barrel common to many different families of glycosyl hydrolases. Structures have been determined for several proteins containing this domain, including family 13 glycosyl hydrolases (such as alpha-amylase) [5], beta-glycanases [6], family 1 glycosyl hydrolases (such as beta-glucosidase) [7], type II chitinases [8], 1,4-beta-N-acetylmuraminidases [9], and beta-N-acetylhexosaminidases [10].
More information about this protein can be found at Protein of the Month: alpha-Amylase [11].
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Structural links
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SCOP:
b.1.18.2
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b.1.4.1
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b.71.1.2
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c.1.8.1
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c.1.8.10
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c.1.8.11
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c.1.8.14
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c.1.8.3
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c.1.8.4
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c.1.8.5
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c.1.8.6
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c.1.8.8
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d.26.3.1
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Example proteins
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O35744 Chitinase-3-like protein 3
P04062 Glucosylceramidase
P23776 Glucan 1,3-beta-glucosidase I/II
P49713 Putative alpha-L-fucosidase
Q9V3D4 Chitinase-like protein Idgf2
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR016286 |
Glycoside hydrolase, family 29, subgroup |
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| IPR013781 |
Glycoside hydrolase, subgroup, catalytic core |
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| IPR001547 |
Glycoside hydrolase, family 5 |
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| IPR015520 |
Imaginal disc growth factor |
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| IPR018526 |
Glycoside hydrolase, family 29, conserved site |
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| IPR000933 |
Glycoside hydrolase, family 29 |
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| IPR001139 |
Glycoside hydrolase, family 30 |
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| IPR017853 |
Glycoside hydrolase, catalytic core |
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| IPR011583 |
Chitinase II |
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| IPR018087 |
Glycoside hydrolase, family 5, conserved site |
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| IPR001223 |
Glycoside hydrolase, family 18, catalytic domain |
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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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Rydberg EH, Li C, Maurus R, Overall CM, Brayer GD, Withers SG.
Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids.
Biochemistry 41 4492-502 2002
[PubMed: 11914097]
http://dx.doi.org/10.1021/bi011821z
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6.
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Pell G, Taylor EJ, Gloster TM, Turkenburg JP, Fontes CM, Ferreira LM, Nagy T, Clark SJ, Davies GJ, Gilbert HJ.
The mechanisms by which family 10 glycoside hydrolases bind decorated substrates.
J. Biol. Chem. 279 9597-605 2004
[PubMed: 14668328]
http://dx.doi.org/10.1074/jbc.M312278200
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7.
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Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B.
High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base.
J. Biol. Chem. 275 39385-93 2000
[PubMed: 10978344]
http://dx.doi.org/10.1074/jbc.M006796200
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8.
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Bokma E, Rozeboom HJ, Sibbald M, Dijkstra BW, Beintema JJ.
Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis.
Eur. J. Biochem. 269 893-901 2002
[PubMed: 11846790]
http://dx.doi.org/10.1046/j.0014-2956.2001.02721.x
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9.
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Rau A, Hogg T, Marquardt R, Hilgenfeld R.
A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution.
J. Biol. Chem. 276 31994-9 2001
[PubMed: 11427528]
http://dx.doi.org/10.1074/jbc.M102591200
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10.
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Williams SJ, Mark BL, Vocadlo DJ, James MN, Withers SG.
Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state.
J. Biol. Chem. 277 40055-65 2002
[PubMed: 12171933]
http://dx.doi.org/10.1074/jbc.M206481200
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11.
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Mcdowall A.
Protein of the Month ? alpha-Amylase.
2006
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Additional Reading
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Maurus R, Begum A, Williams LK, Fredriksen JR, Zhang R, Withers SG, Brayer GD.
Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity.
Biochemistry 47 2008 3332-44
[PubMed: 18284212]
http://dx.doi.org/10.1021/bi701652t
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Aguilar M, Gloster TM, Garcia-Moreno MI, Ortiz Mellet C, Davies GJ, Llebaria A, Casas J, Egido-Gabas M, Garcia Fernandez JM.
Molecular basis for beta-glucosidase inhibition by ring-modified calystegine analogues.
Chembiochem 9 2008 2612-8
[PubMed: 18833549]
http://dx.doi.org/10.1002/cbic.200800451
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Chuenchor W, Pengthaisong S, Robinson RC, Yuvaniyama J, Oonanant W, Bevan DR, Esen A, Chen CJ, Opassiri R, Svasti J, Cairns JR.
Structural insights into rice BGlu1 beta-glucosidase oligosaccharide hydrolysis and transglycosylation.
J. Mol. Biol. 377 2008 1200-15
[PubMed: 18308333]
http://dx.doi.org/10.1016/j.jmb.2008.01.076
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Sharma P, Singh N, Sinha M, Sharma S, Perbandt M, Betzel C, Kaur P, Srinivasan A, Singh TP.
Tryptophan as a three-way switch in regulating the function of the secretory signalling glycoprotein (SPS-40) from mammary glands: structure of SPS-40 complexed with 2-methylpentane-2,4-diol at 1.6 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 65 2009 375-8
[PubMed: 19307719]
http://dx.doi.org/10.1107/S0907444909002327
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Tailford LE, Offen WA, Smith NL, Dumon C, Morland C, Gratien J, Heck MP, Stick RV, Bleriot Y, Vasella A, Gilbert HJ, Davies GJ.
Structural and biochemical evidence for a boat-like transition state in beta-mannosidases.
Nat. Chem. Biol. 4 2008 306-12
[PubMed: 18408714]
http://dx.doi.org/10.1038/nchembio.81
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