spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR008960 Carbohydrate-binding domain family 9-like

Protein matchesHelp
UniProtKB
Matches:
625 proteins
AccessionHelp IPR008960 Carb-bd_dom_fam9-like
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR015920 Cellobiose dehydrogenase, cytochrome
IPR015922 Carbohydrate-binding domain, family 9-like, subgroup
GO Term annotationHelp
Process GO:0016052 carbohydrate catabolic process
Function GO:0003824 catalytic activity
GO:0030246 carbohydrate binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents an immunoglobulin-like beta-sandwich domain found in a variety of protein families, including family 9 carbohydrate-binding (CDB9) enzymes like endo-1,4-beta-xylanase (EC:3.2.1.8), as the C-terminal domain of glucodextranase enzymes (EC:3.2.1.70), and as the cytochrome domain of cellobiose dehydrogenase enzymes (EC:1.1.99.18). In general, these domains consist of 7 beta-strands in 2 sheets with a Greek key topology, but with an additional beta-strand at the N terminus [1, 2].

Bacterial extracellular cellulases and hemicellulases are involved in the hydrolysis of the major structural polysaccharides of plant cell walls. These are usually modular enzymes that contain catalytic and non-catalytic domains. The CBD9 domain binds to cellulose, xylan, as well as to a range of soluble di- and mono-saccharides, and is found in cellulose- and xylan-degrading enzymes [3].

Cellobiose dehydrogenases (CDHs) are extracellular hemoflavoenzymes produced by various wood-degrading fungi that are involved in the degradation of cellulose and lignin [4]. These enzymes consist of a cytochrome domain and a flavin domain, which are believed to have evolved in parallel as fused genes, because the two domains can be cleaved proteolytically to make a functional cytochrome and flavodehydrogenase [5]. The b-type cytochrome domain contains a 6-coordinate low spin b-type haem with unusual iron ligands and coordination geometry.

Glucodextranase hydrolyzes alpha-1,6-glucosidic linkages of dextran from the non-reducing end to produce beta-D-glucose via an inverting reaction mechanism and classified into the glycoside hydrolase family 15 (GH15) [6].

Structural linksHelp
SCOP: b.1.9.1 , b.1.9.2 , b.1.9.3

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008960 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
Q01738 Cellobiose dehydrogenase

Q08CS6 DBH-like monooxygenase protein 2 homolog

Q60037 Endo-1,4-beta-xylanase A

Q60QM8 DOMON domain-containing protein CBG21753

Q9XWC3 DOMON domain-containing protein Y73F4A.2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR003305 Carbohydrate-binding, CenC-like
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR010502 Carbohydrate-binding domain, family 9
IPR015922 Carbohydrate-binding domain, family 9-like, subgroup
IPR000945 Dopamine-beta-monooxygenase
IPR007867 Glucose-methanol-choline oxidoreductase, C-terminal
IPR005018 DOMON related
IPR013050 DOMON
IPR014783 Copper type II, ascorbate-dependent monooxygenase, C-terminal
IPR014784 Copper type II, ascorbate-dependent monooxygenase-like, C-terminal
IPR001000 Glycoside hydrolase, family 10
IPR000172 Glucose-methanol-choline oxidoreductase, N-terminal
IPR008977 PHM/PNGase F-fold
IPR008979 Galactose-binding domain-like
IPR017853 Glycoside hydrolase, catalytic core
IPR000323 Copper type II, ascorbate-dependent monooxygenase, N-terminal
IPR015920 Cellobiose dehydrogenase, cytochrome
IPR008960 Carbohydrate-binding domain family 9-like
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Notenboom V, Boraston AB, Kilburn DG, Rose DR.
Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms.
Biochemistry 40 6248-56 2001 [PubMed: 11371186]
http://dx.doi.org/10.1021/bi0101704
2. Rotsaert FA, Hallberg BM, de Vries S, Moenne-Loccoz P, Divne C, Renganathan V, Gold MH.
Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase.
J. Biol. Chem. 278 33224-31 2003 [PubMed: 12796496]
http://dx.doi.org/10.1074/jbc.M302653200
3. Hazlewood GP, Gilbert HJ.
Structure and function analysis of Pseudomonas plant cell wall hydrolases.
Prog. Nucleic Acid Res. Mol. Biol. 61 211-41 1998 [PubMed: 9752722]
4. Henriksson G, Johansson G, Pettersson G.
A critical review of cellobiose dehydrogenases.
J. Biotechnol. 78 93-113 2000 [PubMed: 10725534]
http://dx.doi.org/10.1016/S0168-1656(00)00206-6
5. Hallberg BM, Bergfors T, Backbro K, Pettersson G, Henriksson G, Divne C.
A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase.
Structure 8 79-88 2000 [PubMed: 10673428]
http://dx.doi.org/10.1016/S0969-2126(00)00082-4
6. Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y.
Structural insights into substrate specificity and function of glucodextranase.
J. Biol. Chem. 279 10575-83 2004 [PubMed: 14660574]
http://dx.doi.org/10.1074/jbc.M310771200

spacer
spacer
InterPro 23.1