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Carbohydrate Binding Module Family 74

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Carbohydrate Binding Module Family 74
Carbohydrate Specificity Starch
Associated GH Families GH13_28
CAZy DB link

Ligand specificities

The dialysis refolded MaAmyA CBM74 domain was shown to bind to soluble potato starch, boiled granular potato, wheat, and waxy corn starch (type 3 resistant starches) as well as amylose (unspecified source), and amylopectin (unspecified source) by polysaccharide‐binding macroarray. This domain also binds to raw granular starches (type 2 resistant starch) from potato, wheat, and waxy corn as shown by adsorption depletion. CBM74 showed a higher affinity for potato derived starch over that from wheat and maize suggesting that the CBM74 domain has a higher affinity for starches with A-type crystallinity over B-type [1]

Structural Features

Content in this section should include, in paragraph form, a description of:

  • Fold: Structural fold (beta trefoil, beta sandwich, etc.)
  • Type: Include here Type A, B, or C and properties
  • Features of ligand binding: Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.


Content in this section should include, in paragraph form, a description of:

  • Functional role of CBM: Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
  • Most Common Associated Modules: 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
  • Novel Applications: Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.

Family Firsts

First Identified
CBM74 was first identified as the C-terminal domain of a multi-modular α-amylase, MaAmyA, originating from Microbacterium aurum[1].
First Structural Characterization
No structure has yet been determined for any CBM74 family member.


  1. Valk V, Lammerts van Bueren A, van der Kaaij RM, and Dijkhuizen L. (2016) Carbohydrate-binding module 74 is a novel starch-binding domain associated with large and multidomain α-amylase enzymes. FEBS J. 283, 2354-68. DOI:10.1111/febs.13745 | PubMed ID:27101946 | HubMed [Valk2016]
  2. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 37, D233-8. DOI:10.1093/nar/gkn663 | PubMed ID:18838391 | HubMed [Cantarel2009]
  3. Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.
  4. Boraston AB, Bolam DN, Gilbert HJ, and Davies GJ. (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 382, 769-81. DOI:10.1042/BJ20040892 | PubMed ID:15214846 | HubMed [Boraston2004]
  5. Hashimoto H (2006) Recent structural studies of carbohydrate-binding modules. Cell Mol Life Sci. 63, 2954-67. DOI:10.1007/s00018-006-6195-3 | PubMed ID:17131061 | HubMed [Hashimoto2006]
  6. Shoseyov O, Shani Z, and Levy I. (2006) Carbohydrate binding modules: biochemical properties and novel applications. Microbiol Mol Biol Rev. 70, 283-95. DOI:10.1128/MMBR.00028-05 | PubMed ID:16760304 | HubMed [Shoseyov2006]
  7. Guillén D, Sánchez S, and Rodríguez-Sanoja R. (2010) Carbohydrate-binding domains: multiplicity of biological roles. Appl Microbiol Biotechnol. 85, 1241-9. DOI:10.1007/s00253-009-2331-y | PubMed ID:19908036 | HubMed [Guillen2010]
All Medline abstracts: PubMed | HubMed