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InterPro: IPR017853 Glycoside hydrolase, catalytic core
Protein matches
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UniProtKB Matches: 47864 proteins |
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Accession
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IPR017853 Glyco_hydro_catalytic_core |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR001764 Glycoside hydrolase, family 3, N-terminal
IPR013781 Glycoside hydrolase, subgroup, catalytic core
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Found in
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IPR000111 Glycoside hydrolase, clan GH-D
IPR000322 Glycoside hydrolase, family 31
IPR001329 Glycoside hydrolase, family 56, allergen Api/Dol m 2
IPR001439 Glycoside hydrolase, family 56, sperm surface protein PH20
IPR001968 Glycoside hydrolase, family 56
IPR002241 Glycoside hydrolase, family 27
IPR002252 Glycoside hydrolase, family 36
IPR005199 Glycoside hydrolase family 79, N-terminal
IPR006215 Glycoside hydrolase, melibiase
IPR006407 1,4-alpha-glucan branching enzyme, core region
IPR008589 Protein of unknown function DUF871, prokaryotic
IPR008811 Raffinose synthase
IPR017430 Glycoside hydrolase, family 56, Hyaluronidase
IPR018155 Hyaluronidase
IPR019563 Glycoside hydrolase 97
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Contains
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IPR011099 Glycosyl hydrolase 67, C-terminal
IPR013797 Maltooligosyl trehalose synthase, N-terminal
IPR015020 Domain of unknown function DUF1906
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
IPR019800 Glycoside hydrolase, family 3, active site
IPR019801 Glycoside hydrolase, family 35, conserved site
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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.3.1.1
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b.71.1.1
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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.1.8.12
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c.1.8.13
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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.1.8.7
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c.1.8.8
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c.1.8.9
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d.26.3.1
CATH:
1.10.10.470
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1.10.150.200
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2.60.40.10
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2.60.40.1180
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2.60.40.1500
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2.60.40.320
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3.10.50.10
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3.20.20.300
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3.20.20.70
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3.20.20.80
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3.30.1590.10
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3.90.1330.10
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3.90.400.10
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Example proteins
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O35744
P04062
P23776
P49713
Q9V3D4
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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Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM.
Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin.
Chem. Biol. 15 2008 295-301
[PubMed: 18355729]
http://dx.doi.org/10.1016/j.chembiol.2008.02.015
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