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PROSITE documentation PDOC51763 [for PROSITE entry PS51763]

CBM10 (carbohydrate binding type-10) domain profile





Description

Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs). The majority of these CBMs interact with cellulose and are thus referred to as cellulose-binding domains or CBDs. CBM10s are small molecules, comprising only ca. 45 residues, that bind to insoluble forms of cellulose [E1]. CBM10s contain three tryptophan and two tyrosine residues which are completely conserved. The CBM10 domain is found in xylanases, mannanases and cellulases from aerobic bacteria and anaerobic fungi [1,2,3,4].

The CBM10 domain consists of two antiparallel β-sheets, one with two strands and one with three, with a short α-helix across one face of the three-stranded sheet (see <PDB:1QLD>) [2,4].

Some proteins known to contain a CBM10 domain are listed below:

  • Cellvibrio japonicus endo-1,4-β-xylanase A (xynA), endohydrolyses (1->4)-β-D-xylosidic linkages in xylans.
  • Cellvibrio japonicus bifunctional xylanase/xylan deacetylase (xyn11A), endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides.
  • Cellvibrio japonicus endoglucanase A (celA), endohydrolyses (1->4)-β-D- glucosidic linkages in cellulose, lichenin and cereal β-D-glucans.
  • Cellvibrio japonicus endoglucanase B (celB), catalyzes the endohydrolysis of 1,4-β-glucosidic linkages in cellulose, lichenin and cereal β-D- glucans.
  • Cellvibrio japonicus endoglucanase C (celC), endohydrolyses (1->4)-β-D- glucosidic linkages in cellulose, lichenin and cereal β-D-glucans.
  • Neocallimastix patriciarum (Rumen fungus) endoglucanase B (CELB), endohydrolyse (1->4)-β-D-glucosidic linkages in cellulose, lichenin and cereal β-D-glucans.
  • Neocallimastix patriciarum (Rumen fungus) bifunctional endo-1,4-β- xylanase A (XYNA), hydrolyzes xylans into xylobiose and xylose.
  • Piromyces sp. endo-1,4-β-xylanase A (XYNA), hydrolyzes 1,4-β linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods.
  • Piromyces sp. mannan endo-1,4-β-mannosidase A (MANA), hydrolyzes 1,4- β linked polysaccharide backbones of mannans, one of the major hemicellulose components in hardwoods and softwoods.

The profile we developed covers the entire CBM10 domain.

Last update:

June 2015 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CBM10, PS51763; CBM10 (carbohydrate-binding type-10) domain profile  (MATRIX)


References

1AuthorsPonyi T. Szabo L. Nagy T. Orosz L. Simpson P.J. Williamson M.P. Gilbert H.J.
TitleTrp22, Trp24, and Tyr8 play a pivotal role in the binding of the family 10 cellulose-binding module from Pseudomonas xylanase A to insoluble ligands.
SourceBiochemistry 39:985-991(2000).
PubMed ID10653642

2AuthorsRaghothama S. Simpson P.J. Szabo L. Nagy T. Gilbert H.J. Williamson M.P.
TitleSolution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A.
SourceBiochemistry 39:978-984(2000).
PubMed ID10653641

3AuthorsFanutti C. Ponyi T. Black G.W. Hazlewood G.P. Gilbert H.J.
TitleThe conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain.
SourceJ. Biol. Chem. 270:29314-29322(1995).
PubMed ID7493964

4AuthorsRaghothama S. Eberhardt R.Y. Simpson P. Wigelsworth D. White P. Hazlewood G.P. Nagy T. Gilbert H.J. Williamson M.P.
TitleCharacterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi.
SourceNat. Struct. Biol. 8:775-778(2001).
PubMed ID11524680
DOI10.1038/nsb0901-775

E1Sourcehttp://www.cazy.org/CBM10.html



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