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InterPro: IPR013319 Glycoside hydrolase, family 11/12, catalytic domain

Protein matchesHelp
UniProtKB
Matches:
725 proteins
AccessionHelp IPR013319 Glyco_hydro_11/12_cat
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR008985 Concanavalin A-like lectin/glucanase
Found in IPR001137 Glycoside hydrolase, family 11
IPR002594 Glycoside hydrolase, family 12
Contains IPR018208 Glycoside hydrolase, family 11, active site
GO Term annotationHelp
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 11 GH11 comprises enzymes with only one known activity, xylanase (EC:3.2.1.8), while family 12 GH12 comprises enzymes with two known activities, endoglucanase (EC:3.2.1.4) and xyloglucan hydrolase. This entry represents the catalytic core of family 11 and 12 glycoside hydrolases, which assumes a beta-sandwich structure of complex topology, consisting of 12-14 beta-strands in two sheets.

Structural linksHelp
PDB - click here
SCOP: b.29.1.11
CATH: 2.60.120.180
Database linksHelp
Enzyme: EC:3.2.1.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR013319 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O43097 Endo-1,4-beta-xylanase

O97402 Endo-1,4-beta-xylanase

P09850 Endo-1,4-beta-xylanase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR018208 Glycoside hydrolase, family 11, active site
IPR001137 Glycoside hydrolase, family 11
IPR013319 Glycoside hydrolase, family 11/12, catalytic domain
IPR008985 Concanavalin A-like lectin/glucanase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH 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

Additional ReadingHelp
Vandermarliere E, Bourgois TM, Rombouts S, Van Campenhout S, Volckaert G, Strelkov SV, Delcour JA, Rabijns A, Courtin CM.
Crystallographic analysis shows substrate binding at the -3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-beta-xylanases.
Biochem. J. 410 2008 71-9 [PubMed: 17983355]
http://dx.doi.org/10.1042/BJ20071128
Vardakou M, Dumon C, Murray JW, Christakopoulos P, Weiner DP, Juge N, Lewis RJ, Gilbert HJ, Flint JE.
Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanases.
J. Mol. Biol. 375 2008 1293-305 [PubMed: 18078955]
http://dx.doi.org/10.1016/j.jmb.2007.11.007
Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E.
Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A.
J. Mol. Biol. 356 2006 57-71 [PubMed: 16343530]
http://dx.doi.org/10.1016/j.jmb.2005.11.004
Jiang L, Althoff EA, Clemente FR, Doyle L, Rothlisberger D, Zanghellini A, Gallaher JL, Betker JL, Tanaka F, Barbas CF 3rd, Hilvert D, Houk KN, Stoddard BL, Baker D.
De novo computational design of retro-aldol enzymes.
Science 319 2008 1387-91 [PubMed: 18323453]
http://dx.doi.org/10.1126/science.1152692
Miyatake H, Hasegawa T, Yamano A.
New methods to prepare iodinated derivatives by vaporizing iodine labelling (VIL) and hydrogen peroxide VIL (HYPER-VIL).
Acta Crystallogr. D Biol. Crystallogr. 62 2006 280-9 [PubMed: 16510975]
http://dx.doi.org/10.1107/S0907444905041909
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InterPro 23.1