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InterPro: IPR006584 Cellulose binding, type IV

Protein matchesHelp
UniProtKB
Matches:
321 proteins
AccessionHelp IPR006584 Cellulose_bd_IV
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR005084 Carbohydrate binding domain, family 6
GO Term annotationHelp
Function GO:0030246 carbohydrate binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents a type IV cellulose binding domain. It is a sub-domain of the carbohydrate-binding module, family 6 (GH6).

Regarding the function, it shows endohydrolysis of 1,4-beta-d-xylosidic linkages in xylans [1].

Structural linksHelp
SCOP: b.18.1.10
CATH: 2.60.120.260
Database linksHelp
Enzyme: EC:3.2.1
Blocks: IPB006584

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006584 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P10478 Endo-1,4-beta-xylanase Z

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR016134 Cellulosome enzyme, dockerin type I
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR006584 Cellulose binding, type IV
IPR000801 Putative esterase
IPR005084 Carbohydrate binding domain, family 6
IPR001000 Glycoside hydrolase, family 10
IPR018247 EF-Hand 1, calcium-binding site
IPR008979 Galactose-binding domain-like
IPR002105 Cellulosome enzyme, dockerin type I, calcium-binding motif
IPR017853 Glycoside hydrolase, catalytic core
IPR018242 Dockerin type 1
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Gosalbes MJ, Perez-Gonzalez JA, Gonzalez R, Navarro A.
Two beta-glycanase genes are clustered in Bacillus polymyxa: molecular cloning, expression, and sequence analysis of genes encoding a xylanase and an endo-beta-(1,3)-(1,4)-glucanase.
J. Bacteriol. 173 7705-10 1991 [PubMed: 1938968]
http://jb.asm.org/cgi/content/abstract/173/23/7705

Additional ReadingHelp
Lammerts van Bueren A, Boraston AB.
Binding sub-site dissection of a carbohydrate-binding module reveals the contribution of entropy to oligosaccharide recognition at "non-primary" binding subsites.
J. Mol. Biol. 340 2004 869-79 [PubMed: 15223327]
http://dx.doi.org/10.1016/j.jmb.2004.05.038
Boraston AB, Notenboom V, Warren RA, Kilburn DG, Rose DR, Davies G.
Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and "galactose-binding" domains.
J. Mol. Biol. 327 2003 659-69 [PubMed: 12634060]
http://dx.doi.org/10.1016/S0022-2836(03)00152-9
Czjzek M, Bolam DN, Mosbah A, Allouch J, Fontes CM, Ferreira LM, Bornet O, Zamboni V, Darbon H, Smith NL, Black GW, Henrissat B, Gilbert HJ.
The location of the ligand-binding site of carbohydrate-binding modules that have evolved from a common sequence is not conserved.
J. Biol. Chem. 276 2001 48580-7 [PubMed: 11673472]
http://intl.jbc.org/cgi/content/full/276/51/48580
van Bueren AL, Morland C, Gilbert HJ, Boraston AB.
Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface.
J. Biol. Chem. 280 2005 530-7 [PubMed: 15501830]
http://intl.jbc.org/cgi/reprint/280/1/530.pdf
Pires VM, Henshaw JL, Prates JA, Bolam DN, Ferreira LM, Fontes CM, Henrissat B, Planas A, Gilbert HJ, Czjzek M.
The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5a in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities.
J. Biol. Chem. 279 2004 21560-8 [PubMed: 15010454]
http://dx.doi.org/10.1074/jbc.M401599200
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InterPro 23.1