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InterPro: IPR008965 Carbohydrate-binding

Protein matchesHelp
UniProtKB
Matches:
1358 proteins
AccessionHelp IPR008965 Carb_bd
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR001956 Bacterial type 3a, cellulose-binding
IPR002102 Cellulosome anchoring protein, cohesin domain
IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain
Contains IPR018366 Carbohydrate-binding type-2, conserved site
IPR019028 Carbohydrate binding domain CBM49
GO Term annotationHelp
Function GO:0030246 carbohydrate binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This carbohydrate-binding domain is found in a number of proteins, for example the N-terminal domain of the chitobiase/beta-hexosaminidase family of glycoside hydrolases, the carbohydrate-binding domain of bacterial cellulases and xylanases, and the cellulose-binding domain of bacterial proteins such as scafoldin, cellobiose and cohesin. The carbohydrate-binding domain consists of a beta-sandwich formed of 9 strands in 2 sheets with a Greek-key topology and is a sub-class of the immunoglobin-like fold [1].

Structural linksHelp
SCOP: b.2.2.1 , b.2.2.2 , b.2.2.3
Database linksHelp
Enzyme: EC:3.2.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008965 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P07986 Exoglucanase/xylanase

P08797 Stalk-specific protein A

Q42059 Endoglucanase 6

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR001701 Glycoside hydrolase, family 9
IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain
IPR019028 Carbohydrate binding domain CBM49
IPR012341 Six-hairpin glycosidase
IPR008965 Carbohydrate-binding
IPR001000 Glycoside hydrolase, family 10
IPR008928 Six-hairpin glycosidase-like
IPR017853 Glycoside hydrolase, catalytic core
IPR001919 Cellulose-binding domain, family II, bacterial type
IPR018221 Glycoside hydrolase, family 9, active site
IPR018366 Carbohydrate-binding type-2, conserved site
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, Steitz TA.
Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose.
EMBO J. 15 5739-51 1996 [PubMed: 8918451]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8918451

Additional ReadingHelp
Carvalho AL, Dias FM, Nagy T, Prates JA, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LM, Romao MJ, Fontes CM, Gilbert HJ.
Evidence for a dual binding mode of dockerin modules to cohesins.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 3089-94 [PubMed: 17360613]
http://dx.doi.org/10.1073/pnas.0611173104
Adams JJ, Pal G, Jia Z, Smith SP.
Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 305-10 [PubMed: 16384918]
http://dx.doi.org/10.1073/pnas.0507109103
Noach I, Frolow F, Jakoby H, Rosenheck S, Shimon LW, Lamed R, Bayer EA.
Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements.
J. Mol. Biol. 348 2005 1-12 [PubMed: 15808849]
http://dx.doi.org/10.1016/j.jmb.2005.02.024
Noach I, Frolow F, Alber O, Lamed R, Shimon LJ, Bayer EA.
Intermodular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus.
J. Mol. Biol. 391 2009 86-97 [PubMed: 19501595]
Pinheiro BA, Proctor MR, Martinez-Fleites C, Prates JA, Money VA, Davies GJ, Bayer EA, Fontesm CM, Fierobe HP, Gilbert HJ.
The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner.
J. Biol. Chem. 283 2008 18422-30 [PubMed: 18445585]
http://dx.doi.org/10.1074/jbc.M801533200
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InterPro 23.1