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Carbohydrate-binding module

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Carbohydrate-binding module

three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase i from trichoderma reesei, nmr, 18 structures
Symbol CBM_1
Pfam PF00734
InterPro IPR000254
SCOP 1cel
solution structure of a cellulose binding domain from cellulomonas fimi by nuclear magnetic resonance spectroscopy
Symbol CBM_2
Pfam PF00553
Pfam clan CL0203
InterPro IPR001919
SCOP 1exg
crystal structure of a family iiia cbd from clostridium cellulolyticum
Symbol CBM_3
Pfam PF00942
Pfam clan CL0203
InterPro IPR001956
SCOP 1nbc
interactions of a family 18 chitinase with the designed inhibitor hm508, and its degradation product, chitobiono-delta-lactone
Symbol CBM_5_12
Pfam PF02839
InterPro IPR003610
SCOP 1ed7
cbm6ct from clostridium thermocellum in complex with xylopentaose
Symbol CBM_6
Pfam PF03422
Pfam clan CL0202
InterPro IPR005084
SCOP 1gmm
cbm4 structure and function
Symbol CBM_4_9
Pfam PF02018
Pfam clan CL0202
InterPro IPR003305
SCOP 1ulp
solution structure of type x cbm
Symbol CBM_10
Pfam PF02013
InterPro IPR002883
SCOP 1qld
family 11 carbohydrate-binding module of cellulosomal cellulase lic26a-cel5e of clostridium thermocellum
Symbol CBM_11
Pfam PF03425
Pfam clan CL0202
InterPro IPR005087
Symbol CBM_14
Pfam PF01607
Pfam clan CL0155
InterPro IPR002557
SCOP 1dqc
xylan-binding module cbm15
Symbol CBM_15
Pfam PF03426
Pfam clan CL0202
InterPro IPR005088
SCOP 1gny
structure of fam17 carbohydrate binding module from clostridium cellulovorans
Symbol CBM_17_28
Pfam PF03424
Pfam clan CL0202
InterPro IPR005086
SCOP 1g0c
Chitin_bind_1 (CBM18)
crystal structure analysis of crosslinked-wga3/glcnacbeta1,4glcnac complex
Symbol Chitin_bind_1
Pfam PF00187
InterPro IPR001002
SCOP 1wgt
Symbol CBM_19
Pfam PF03427
Pfam clan CL0155
InterPro IPR005089
glucoamylase, granular starch-binding domain complex with cyclodextrin, nmr, minimized average structure
Symbol CBM_20
Pfam PF00686
Pfam clan CL0369
InterPro IPR002044
SCOP 1cdg
Symbol CBM_21
Pfam PF03370
InterPro IPR005036
Symbol CBM_25
Pfam PF03423
InterPro IPR005085
structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module, tmcbm27
Symbol CBM27
Pfam PF09212
InterPro IPR015295
SCOP 1oh4
Chitin_bind_3 (CBM33)
crystal structure of the serratia marcescens chitin-binding protein cbp21 y54a mutant.
Symbol Chitin_bind_3
Pfam PF03067
InterPro IPR004302
crystal structure of glycosyltrehalose trehalohydrolase from sulfolobus solfataricus
Symbol CBM_48
Pfam PF02922
Pfam clan CL0369
InterPro IPR004193
SCOP 1bf2
Symbol CBM49
Pfam PF09478
Pfam clan CL0203
InterPro IPR019028

In molecular biology, a carbohydrate-binding module (CBM) is a protein domain found in carbohydrate-active enzymes (for example glycoside hydrolases). The majority of these domains have carbohydrate-binding activity. Some of these domains are found on cellulosomal scaffoldin proteins. CBMs were previously known as cellulose-binding domains.[1] CBMs are classified into numerous families, based on amino acid sequence similarity. There are currently (June 2011) 64 families of CBM in the CAZy database.[2]

CBMs of microbial glycoside hydrolases play a central role in the recycling of photosynthetically fixed carbon through their binding to specific plant structural polysaccharides.[3] CBMs can recognise both crystalline and amorphous cellulose forms.[4] CBMs are the most common non-catalytic modules associated with enzymes active in plant cell-wall hydrolysis. Many putative CBMs have been identified by amino acid sequence alignments but only a few representatives have been shown experimentally to have a carbohydrate-binding function.[5]


  • CBM1 1
  • CBM2 2
  • CBM3 3
  • CBM4 4
  • CBM5 5
  • CBM6 6
  • CBM9 7
  • CBM10 8
  • CBM11 9
  • CBM12 10
  • CBM14 11
  • CBM15 12
  • CBM17 13
  • CBM18 14
  • CBM19 15
  • CBM20 16
  • CBM21 17
  • CBM25 18
  • CBM27 19
  • CBM28 20
  • CBM33 21
  • CBM48 22
  • CBM49 23
  • References 24
  • External links 25


Carbohydrate-binding module family 1 (CBM1) consists of 36 amino acids. This domain contains 4 conserved cysteine residues which are involved in the formation of two disulfide bonds.


Carbohydrate-binding module family 2 (CBM2) contains two conserved cysteines - one at each extremity of the domain - which have been shown [6] to be involved in a disulfide bond. There are also four conserved tryptophans, two of which are involved in cellulose binding.[7][8][9]


Carbohydrate-binding module family 3 (CBM3) is involved in cellulose binding [10] and is found associated with a wide range of bacterial glycosyl hydrolases. The structure of this domain is known; it forms a beta sandwich.[11]


Carbohydrate-binding module family 4 (CBM4) includes the two cellulose-binding domains, CBD(N1) and CBD(N2), arranged in tandem at the N terminus of the 1,4-beta-glucanase, CenC, from Cellulomonas fimi. These homologous CBMs are distinct in their selectivity for binding amorphous and not crystalline cellulose.[12] Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of the 152 amino acid N-terminal cellulose-binding domain from C. fimi 1,4-beta-glucanase CenC (CBDN1). The tertiary structure of CBDN1 is strikingly similar to that of the bacterial 1,3-1,4-beta-glucanases, as well as other sugar-binding proteins with jelly-roll folds.[13] CBM4 and CBM9 are closely related.


Carbohydrate-binding module family 5 (CBM5) binds chitin.[14] CBM5 and CBM12 are distantly related.


Carbohydrate-binding module family 6 (CBM6) is unusual in that is contains two substrate-binding sites, cleft A and cleft B. Cellvibrio mixtus endoglucanase 5A contains two CBM6 domains, the CBM6 domain at the C-terminus displays distinct ligand binding specificities in each of the sustrate-binding clefts. Both cleft A and cleft B can bind cello-oligosaccharides, laminarin preferentially binds in cleft A, xylooligosaccharides only bind in cleft A and beta1,4,-beta1,3-mixed linked glucans only bind in cleft B.[15]


Carbohydrate-binding module family 9 (CBM9) binds to crystalline cellulose.[16] CBM4 and CBM9 are closely related.


Carbohydrate-binding module family 10 (CBM10) is found in two distinct sets of proteins with different functions. Those found in aerobic bacteria bind cellulose (or other carbohydrates); but in anaerobic fungi they are protein binding domains, referred to as dockerin domains. The dockerin domains are believed to be responsible for the assembly of a multiprotein cellulase/hemicellulase complex, similar to the cellulosome found in certain anaerobic bacteria.[17][18]

In anaerobic bacterial and fungal enzymes are completely different.[19] For example, the fungal enzymes contain one, two or three copies of the dockerin sequence in tandem within the catalytic polypeptide. In contrast, all the C. thermocellum cellulosome catalytic components contain a single dockerin domain. The anaerobic bacterial dockerins are homologous to EF hands (calcium-binding motifs) and require calcium for activity whereas the fungal dockerin does not require calcium. Finally, the interaction between cohesin and dockerin appears to be species specific in bacteria, there is almost no species specificity of binding within fungal species and no identified sites that distinguish different species.

The of dockerin from P. equi contains two helical stretches and four short beta-strands which form an antiparallel sheet structure adjacent to an additional short twisted parallel strand. The N- and C-termini are adjacent to each other.[19]


Carbohydrate-binding module family 11 (CBM11) is found in a number of bacterial cellulases. One example is the CBM11 of Clostridium thermocellum Cel26A-Cel5E, this domain has been shown to bind both β-1,4-glucan and β-1,3-1,4-mixed linked glucans.[20] CBM11 has beta-sandwich structure with a concave side forming a substrate-binding cleft.[20]


Carbohydrate-binding module family 12 (CBM12) comprises two beta-sheets, consisting of two and three antiparallel beta strands respectively. It binds chitin via the aromatic rings of tryptophan residues.[14] CBM5 and CBM12 are distantly related.


Carbohydrate-binding module family 14 (CBM14) is also known as the peritrophin-A domain. It is found in chitin binding proteins, particularly the peritrophic matrix proteins of insects and animal chitinases.[21][22][23] Copies of the domain are also found in some baculoviruses. It is an extracellular domain that contains six conserved cysteines that probably form three disulfide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.[21]


Carbohydrate-binding module family 15 (CBM15), found in bacterial enzymes, has been shown to bind to xylan and xylooligosaccharides. It has a beta-jelly roll fold, with a groove on the concave surface of one of the beta-sheets.[24]


Carbohydrate-binding module family 17 (CBM17) appears to have a very shallow binding cleft that may be more accessible to cellulose chains in non-crystalline cellulose than the deeper binding clefts of family 4 CBMs.[25] Sequence and structural conservation in families CBM17 and CBM28 suggests that they have evolved through gene duplication and subsequent divergence.[4] CBM17 does not compete with CBM28 modules when binding to non-crystalline cellulose. Different CBMs have been shown to bind to different sirtes in amorphous cellulose, CBM17 and CBM28 recognise distinct non-overlapping sites in amorphous cellulose.[26]


Carbohydrate-binding module family 18 (CBM18) (also known as chitin binding 1 or chitin recognition protein) is found in a number of plant and fungal proteins that bind N-acetylglucosamine (e.g. solanaceous lectins of tomato and potato, plant endochitinases, the wound-induced proteins: hevein, win1 and win2, and the Kluyveromyces lactis killer toxin alpha subunit).[27] The domain may occur in one or more copies and is thought to be involved in recognition or binding of chitin subunits.[28][29] In chitinases, as well as in the potato wound-induced proteins, this 43-residue domain directly follows the signal sequence and is therefore at the N terminus of the mature protein; in the killer toxin alpha subunit it is located in the central section of the protein.


Carbohydrate-binding module family 19 (CBM19), found in fungal chitinases, binds chitin.[30]


Carbohydrate-binding module family 20 (CBM20) binds to starch.[31][32]


Carbohydrate-binding module family 21 (CBM21), found in many eukaryotic proteins involved in glycogen metabolism, binds to glycogen.[33]


Carbohydrate-binding module family 25 (CBM25) binds alpha-glucooligosaccharides, particularly those containing alpha-1,6 linkages, and granular starch.[34]


Carbohydrate-binding module family 27 (CBM27) binds to beta-1,4-mannooligosaccharides, carob galactomannan, and konjac glucomannan, but not to cellulose (insoluble and soluble) or soluble birchwood xylan. CBM27 adopts a beta sandwich structure comprising 13 beta strands with a single, small alpha-helix and a single metal atom.[35]


Carbohydrate-binding module family 28 (CBM28) does not compete with CBM17 modules when binding to non-crystalline cellulose. Different CBMs have been shown to bind to different sirtes in amorphous cellulose, CBM17 and CBM28 recognise distinct non-overlapping sites in amorphous cellulose. CBM28 has a "beta-jelly roll" topology, which is similar in structure to the CBM17 domains. Sequence and structural conservation in families CBM17 and CBM28 suggests that they have evolved through gene duplication and subsequent divergence.[4][26]


Carbohydrate-binding module family 33 (CBM33) is a chitin-binding domain.[36] It has a budded fibronectin type III fold consisting of two beta-sheets, arranged as a beta-sheet sandwich and a bud consisting of three short helices, located between beta-strands 1 and 2. It binds chitin via conserved polar amino acids.[37] This domain is found in isolation in baculoviral spheroidin and spindolin proteins.


Carbohydrate-binding module family 48 (CBM48) is often found in enzymes containing glycosyl hydrolase family 13 catalytic domains. It is found in a range of enzymes that act on branched substrates i.e. isoamylase, pullulanase and branching enzyme. Isoamylase hydrolyses 1,6-alpha-D-glucosidic branch linkages in glycogen, amylopectin and dextrin; 1,4-alpha-glucan branching enzyme functions in the formation of 1,6-glucosidic linkages of glycogen; and pullulanase is a starch-debranching enzyme. CBM48 binds glycogen.[38][39][40][41]


Carbohydrate-binding module family 49 (CBM49) is found at the C-terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose.[42]


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External links

  • CAZy Carbohydrate binding modules

This article incorporates text from the public domain Pfam and InterPro IPR000254

This article incorporates text from the public domain Pfam and InterPro IPR002883

This article incorporates text from the public domain Pfam and InterPro IPR005087

This article incorporates text from the public domain Pfam and InterPro IPR002557

This article incorporates text from the public domain Pfam and InterPro IPR005088

This article incorporates text from the public domain Pfam and InterPro IPR005086

This article incorporates text from the public domain Pfam and InterPro IPR005089

This article incorporates text from the public domain Pfam and InterPro IPR001919

This article incorporates text from the public domain Pfam and InterPro IPR002044

This article incorporates text from the public domain Pfam and InterPro IPR005036

This article incorporates text from the public domain Pfam and InterPro IPR005085

This article incorporates text from the public domain Pfam and InterPro IPR015295

This article incorporates text from the public domain Pfam and InterPro IPR001956

This article incorporates text from the public domain Pfam and InterPro IPR004193

This article incorporates text from the public domain Pfam and InterPro IPR019028

This article incorporates text from the public domain Pfam and InterPro IPR003305

This article incorporates text from the public domain Pfam and InterPro IPR003610

This article incorporates text from the public domain Pfam and InterPro IPR005084

This article incorporates text from the public domain Pfam and InterPro IPR001002

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