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0  structures 161  species 0  interactions 801  sequences 38  architectures

Family: CBM49 (PF09478)

Summary: Carbohydrate binding domain CBM49

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Carbohydrate-binding module Edit Wikipedia article

PDB 1azj EBI.jpg
three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase i from trichoderma reesei, nmr, 18 structures
PDB 1exg EBI.jpg
solution structure of a cellulose binding domain from cellulomonas fimi by nuclear magnetic resonance spectroscopy
Pfam clanCL0203
PDB 1g43 EBI.jpg
crystal structure of a family iiia cbd from clostridium cellulolyticum
Pfam clanCL0203
PDB 1ur9 EBI.jpg
interactions of a family 18 chitinase with the designed inhibitor hm508, and its degradation product, chitobiono-delta-lactone
PDB 1uxx EBI.jpg
cbm6ct from clostridium thermocellum in complex with xylopentaose
Pfam clanCL0202
PDB 1gui EBI.jpg
cbm4 structure and function
Pfam clanCL0202
PDB 1qld EBI.jpg
solution structure of type x cbm
PDB 1v0a EBI.jpg
family 11 carbohydrate-binding module of cellulosomal cellulase lic26a-cel5e of clostridium thermocellum
Pfam clanCL0202
Pfam clanCL0155
PDB 1gny EBI.jpg
xylan-binding module cbm15
Pfam clanCL0202
PDB 1j83 EBI.jpg
structure of fam17 carbohydrate binding module from clostridium cellulovorans
Pfam clanCL0202
Chitin_bind_1 (CBM18)
PDB 1k7u EBI.jpg
crystal structure analysis of crosslinked-wga3/glcnacbeta1,4glcnac complex
Pfam clanCL0155
PDB 1ac0 EBI.jpg
glucoamylase, granular starch-binding domain complex with cyclodextrin, nmr, minimized average structure
Pfam clanCL0369
PDB 1of3 EBI.jpg
structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module, tmcbm27
Chitin_bind_3 (CBM33)
PDB 2ben EBI.jpg
crystal structure of the serratia marcescens chitin-binding protein cbp21 y54a mutant.
PDB 1eha EBI.jpg
crystal structure of glycosyltrehalose trehalohydrolase from sulfolobus solfataricus
Pfam clanCL0369
Pfam clanCL0203

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]


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 bacteria that degrade plant cell walls, exemplified by Clostridium thermocellum, the dockerin domains of the catalytic polypeptides can bind equally well to any cohesin from the same organism. More recently, anaerobic fungi, typified by Piromyces equi, have been suggested to also synthesise a cellulosome complex, although the dockerin sequences of the 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.[3]


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.[24] 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.[25]


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).[26] The domain may occur in one or more copies and is thought to be involved in recognition or binding of chitin subunits.[27][28] 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.[29]


Carbohydrate-binding module family 20 (CBM20) binds to starch.[30][31]


Carbohydrate-binding module family 21 (CBM21), found in many eukaryotic proteins involved in glycogen metabolism, binds to glycogen.[32]


Carbohydrate-binding module family 25 (CBM25) binds alpha-glucooligosaccharides, particularly those containing alpha-1,6 linkages, and granular starch.[33]


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.[34]


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][25]


Carbohydrate-binding module family 32 (CBM32) binds to diverse substrates, ranging from plant cell wall polysaccharides to complex glycans.[35] The module has so far been found in microorganisms, including archea, eubacteria and fungi.[35] CBM32 adopts a beta-sandwich fold and has a bound metal atom, most often observed to be calcium.[36] CBM32 modules are associated with catalytic modules such as sialidases, B-N-acetylglucosaminidases, α-N-acetylglucosaminidases, mannanases and galactose oxidases.[36]


Carbohydrate-binding module family 33 (CBM33) is a chitin-binding domain.[37] 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.[38] 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.[39][40][41][42]


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.[43]


  1. ^ Gilkes NR, Henrissat B, Kilburn DG, Miller RC, Warren RA (June 1991). "Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families". Microbiol. Rev. 55 (2): 303–15. PMC 372816. PMID 1886523.
  2. ^ Cantarel, B. L.; Coutinho, P. M.; Rancurel, C.; Bernard, T.; Lombard, V.; Henrissat, B. (2009). "The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics". Nucleic Acids Research. 37 (Database issue): D233–D238. doi:10.1093/nar/gkn663. PMC 2686590. PMID 18838391.
  3. ^ a b Szabo, L.; Jamal, S.; Xie, H.; Charnock, S. J.; Bolam, D. N.; Gilbert, H. J.; Davies, G. J. (2001). "Structure of a Family 15 Carbohydrate-binding Module in Complex with Xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation". Journal of Biological Chemistry. 276 (52): 49061–49065. doi:10.1074/jbc.M109558200. PMID 11598143.
  4. ^ a b c Jamal S, Nurizzo D, Boraston AB, Davies GJ (May 2004). "X-ray crystal structure of a non-crystalline cellulose-specific carbohydrate-binding module: CBM28". J. Mol. Biol. 339 (2): 253–8. doi:10.1016/j.jmb.2004.03.069. PMID 15136030.
  5. ^ Roske Y, Sunna A, Pfeil W, Heinemann U (July 2004). "High-resolution crystal structures of Caldicellulosiruptor strain Rt8B.4 carbohydrate-binding module CBM27-1 and its complex with mannohexaose". J. Mol. Biol. 340 (3): 543–54. doi:10.1016/j.jmb.2004.04.072. PMID 15210353.
  6. ^ Gilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC (December 1991). "Structural and functional relationships in two families of beta-1,4-glycanases". Eur. J. Biochem. 202 (2): 367–77. doi:10.1111/j.1432-1033.1991.tb16384.x. PMID 1761039.
  7. ^ Meinke A, Gilkes NR, Kilburn DG, Miller RC, Warren RA (December 1991). "Bacterial cellulose-binding domain-like sequences in eucaryotic polypeptides". Protein Seq. Data Anal. 4 (6): 349–53. PMID 1812490.
  8. ^ Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP (December 2000). "The structural basis for the ligand specificity of family 2 carbohydrate-binding modules". J. Biol. Chem. 275 (52): 41137–42. doi:10.1074/jbc.M006948200. PMID 10973978.
  9. ^ Xu, G. Y.; Ong, E.; Gilkes, N. R.; Kilburn, D. G.; Muhandiram, D. R.; Harris-Brandts, M.; Carver, J. P.; Kay, L. E.; Harvey, T. S. (1995). "Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy". Biochemistry. 34 (21): 6993–7009. doi:10.1021/bi00021a011. PMID 7766609.
  10. ^ Poole DM, Morag E, Lamed R, Bayer EA, Hazlewood GP, Gilbert HJ (December 1992). "Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS". FEMS Microbiol. Lett. 78 (2–3): 181–6. doi:10.1016/0378-1097(92)90022-g. PMID 1490597.
  11. ^ Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, Steitz TA (November 1996). "Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose". EMBO J. 15 (21): 5739–51. doi:10.1002/j.1460-2075.1996.tb00960.x. PMC 452321. PMID 8918451.
  12. ^ Brun E, Johnson PE, Creagh AL, Tomme P, Webster P, Haynes CA, McIntosh LP (March 2000). "Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C". Biochemistry. 39 (10): 2445–58. doi:10.1021/bi992079u. PMID 10704194.
  13. ^ Johnson PE, Joshi MD, Tomme P, Kilburn DG, McIntosh LP (November 1996). "Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy". Biochemistry. 35 (45): 14381–94. doi:10.1021/bi961612s. PMID 8916925.
  14. ^ a b Akagi, K. -I.; Watanabe, J.; Hara, M.; Kezuka, Y.; Chikaishi, E.; Yamaguchi, T.; Akutsu, H.; Nonaka, T.; Watanabe, T.; Ikegami, T. (2006). "Identification of the Substrate Interaction Region of the Chitin-Binding Domain of Streptomyces griseus Chitinase C". Journal of Biochemistry. 139 (3): 483–493. doi:10.1093/jb/mvj062. PMID 16567413.
  15. ^ Henshaw, J. L.; Bolam, D. N.; Pires, V. M.; Czjzek, M.; Henrissat, B.; Ferreira, L. M.; Fontes, C. M.; Gilbert, H. J. (2004). "The Family 6 Carbohydrate Binding Module CmCBM6-2 Contains Two Ligand-binding Sites with Distinct Specificities". Journal of Biological Chemistry. 279 (20): 21552–21559. doi:10.1074/jbc.M401620200. PMID 15004011.
  16. ^ Winterhalter, C.; Heinrich, P.; Candussio, A.; Wich, G.; Liebl, W. (1995). "Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima". Molecular Microbiology. 15 (3): 431–444. doi:10.1111/j.1365-2958.1995.tb02257.x. PMID 7783614.
  17. ^ Millward-Sadler SJ, Davidson K, Hazlewood GP, Black GW, Gilbert HJ, Clarke JH (November 1995). "Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus". Biochem. J. 312 (1): 39–48. doi:10.1042/bj3120039. PMC 1136224. PMID 7492333.
  18. ^ Fanutti C, Ponyi T, Black GW, Hazlewood GP, Gilbert HJ (December 1995). "The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain". J. Biol. Chem. 270 (49): 29314–22. doi:10.1074/jbc.270.49.29314. PMID 7493964.
  19. ^ a b Raghothama S, Eberhardt RY, Simpson P, Wigelsworth D, White P, Hazlewood GP, Nagy T, Gilbert HJ, Williamson MP (September 2001). "Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi". Nat. Struct. Biol. 8 (9): 775–8. doi:10.1038/nsb0901-775. PMID 11524680.
  20. ^ a b Carvalho, A. L.; Goyal, A.; Prates, J. A.; Bolam, D. N.; Gilbert, H. J.; Pires, V. M.; Ferreira, L. M.; Planas, A.; Romão, M. J.; Fontes, C. M. (2004). "The Family 11 Carbohydrate-binding Module of Clostridium thermocellum Lic26A-Cel5E Accommodates -1,4- and -1,3-1,4-Mixed Linked Glucans at a Single Binding Site". Journal of Biological Chemistry. 279 (33): 34785–34793. doi:10.1074/jbc.M405867200. PMID 15192099.
  21. ^ a b Shen Z, Jacobs-Lorena M (July 1998). "A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression, and characterization". J. Biol. Chem. 273 (28): 17665–70. doi:10.1074/jbc.273.28.17665. PMID 9651363.
  22. ^ Elvin CM, Vuocolo T, Pearson RD, East IJ, Riding GA, Eisemann CH, Tellam RL (April 1996). "Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina. cDNA and deduced amino acid sequences". J. Biol. Chem. 271 (15): 8925–35. doi:10.1074/jbc.271.15.8925. PMID 8621536.
  23. ^ Casu R, Eisemann C, Pearson R, Riding G, East I, Donaldson A, Cadogan L, Tellam R (August 1997). "Antibody-mediated inhibition of the growth of larvae from an insect causing cutaneous myiasis in a mammalian host". Proc. Natl. Acad. Sci. U.S.A. 94 (17): 8939–44. doi:10.1073/pnas.94.17.8939. PMC 22971. PMID 9256413.
  24. ^ Notenboom V, Boraston AB, Chiu P, Freelove AC, Kilburn DG, Rose DR (December 2001). "Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study". J. Mol. Biol. 314 (4): 797–806. doi:10.1006/jmbi.2001.5153. PMID 11733998.
  25. ^ a b Jamal, S.; Nurizzo, D.; Boraston, A. B.; Davies, G. J. (2004). "X-ray Crystal Structure of a Non-crystalline Cellulose-specific Carbohydrate-binding Module: CBM28". Journal of Molecular Biology. 339 (2): 253–258. doi:10.1016/j.jmb.2004.03.069. PMID 15136030.
  26. ^ Wright HT, Sandrasegaram G, Wright CS (September 1991). "Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin". J. Mol. Evol. 33 (3): 283–94. doi:10.1007/bf02100680. PMID 1757999.
  27. ^ Butler AR, O'Donnell RW, Martin VJ, Gooday GW, Stark MJ (July 1991). "Kluyveromyces lactis toxin has an essential chitinase activity". Eur. J. Biochem. 199 (2): 483–8. doi:10.1111/j.1432-1033.1991.tb16147.x. PMID 2070799.
  28. ^ Lerner DR, Raikhel NV (June 1992). "The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase". J. Biol. Chem. 267 (16): 11085–91. PMID 1375935.
  29. ^ Kuranda, M. J.; Robbins, P. W. (1991). "Chitinase is required for cell separation during growth of Saccharomyces cerevisiae". The Journal of Biological Chemistry. 266 (29): 19758–19767. PMID 1918080.
  30. ^ Penninga, D.; Van Der Veen, B. A.; Knegtel, R. M.; Van Hijum, S. A.; Rozeboom, H. J.; Kalk, K. H.; Dijkstra, B. W.; Dijkhuizen, L. (1996). "The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251". The Journal of Biological Chemistry. 271 (51): 32777–32784. doi:10.1074/jbc.271.51.32777. PMID 8955113.
  31. ^ Oyama, T.; Kusunoki, M.; Kishimoto, Y.; Takasaki, Y.; Nitta, Y. (1999). "Crystal structure of beta-amylase from Bacillus cereus var. Mycoides at 2.2 a resolution". Journal of Biochemistry. 125 (6): 1120–1130. doi:10.1093/oxfordjournals.jbchem.a022394. PMID 10348915.
  32. ^ Armstrong, C. G.; Doherty, M. J.; Cohen, P. T. (1998). "Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1". The Biochemical Journal. 336 (3): 699–704. doi:10.1042/bj3360699. PMC 1219922. PMID 9841883.
  33. ^ Boraston, A. B.; Healey, M.; Klassen, J.; Ficko-Blean, E.; Lammerts Van Bueren, A.; Law, V. (2005). "A Structural and Functional Analysis of -Glucan Recognition by Family 25 and 26 Carbohydrate-binding Modules Reveals a Conserved Mode of Starch Recognition". Journal of Biological Chemistry. 281 (1): 587–598. doi:10.1074/jbc.M509958200. PMID 16230347.
  34. ^ Boraston AB, Revett TJ, Boraston CM, Nurizzo D, Davies GJ (June 2003). "Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, TmCBM27". Structure. 11 (6): 665–75. doi:10.1016/S0969-2126(03)00100-X. PMID 12791255.
  35. ^ a b Abbot, DW; Eirin-Lopez, JM; Boraston, AB (January 2008). "Insight into ligand diversity and novel biological roles for family 32 carbohydrate-binding modules". Molecular Biology and Evolution. 25 (1): 155–67. doi:10.1093/molbev/msm243. PMID 18032406.
  36. ^ a b Ficko-Blean, Elizabeth; Boraston, Alisdair ,"Carbohydrate Binding Module Family 32" Archived 2016-08-20 at the Wayback Machine,CAZypedia, 4 May 2017.
  37. ^ Schnellmann, J.; Zeltins, A.; Blaak, H.; Schrempf, H. (1994). "The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline alpha-chitin of fungi and other organisms". Molecular Microbiology. 13 (5): 807–819. doi:10.1111/j.1365-2958.1994.tb00473.x. PMID 7815940.
  38. ^ Vaaje-Kolstad, G.; Houston, D. R.; Riemen, A. H.; Eijsink, V. G.; Van Aalten, D. M. (2005). "Crystal Structure and Binding Properties of the Serratia marcescens Chitin-binding Protein CBP21". Journal of Biological Chemistry. 280 (12): 11313–11319. doi:10.1074/jbc.M407175200. PMID 15590674.
  39. ^ Katsuya, Y.; Mezaki, Y.; Kubota, M.; Matsuura, Y. (1998). "Three-dimensional structure of Pseudomonas isoamylase at 2.2 Ã… resolution1". Journal of Molecular Biology. 281 (5): 885–897. doi:10.1006/jmbi.1998.1992. PMID 9719642.
  40. ^ Wiatrowski, H. A.; Van Denderen, B. J.; Berkey, C. D.; Kemp, B. E.; Stapleton, D.; Carlson, M. (2004). "Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism". Molecular and Cellular Biology. 24 (1): 352–361. doi:10.1128/mcb.24.1.352-361.2004. PMC 303368. PMID 14673168.
  41. ^ Polekhina, G.; Gupta, A.; Michell, B. J.; Van Denderen, B.; Murthy, S.; Feil, S. C.; Jennings, I. G.; Campbell, D. J.; Witters, L. A.; Parker, M. W.; Kemp, B. E.; Stapleton, D. (2003). "AMPK beta subunit targets metabolic stress sensing to glycogen". Current Biology. 13 (10): 867–871. doi:10.1016/S0960-9822(03)00292-6. PMID 12747837.
  42. ^ Hudson, E. R.; Pan, D. A.; James, J.; Lucocq, J. M.; Hawley, S. A.; Green, K. A.; Baba, O.; Terashima, T.; Hardie, D. G. (2003). "A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias". Current Biology. 13 (10): 861–866. doi:10.1016/S0960-9822(03)00249-5. PMID 12747836.
  43. ^ Urbanowicz BR, Catala C, Irwin D, Wilson DB, Ripoll DR, Rose JK (April 2007). "A tomato endo-beta-1,4-glucanase, SlCel9C1, represents a distinct subclass with a new family of carbohydrate binding modules (CBM49)". J. Biol. Chem. 282 (16): 12066–74. doi:10.1074/jbc.M607925200. PMID 17322304.

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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
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This article incorporates text from the public domain Pfam and InterPro: IPR005088
This article incorporates text from the public domain Pfam and InterPro: IPR005086
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This article incorporates text from the public domain Pfam and InterPro: IPR001919
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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

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Carbohydrate binding domain CBM49 Provide feedback

This domain is found at the C terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose [1].

Literature references

  1. Urbanowicz BR, Catala C, Irwin D, Wilson DB, Ripoll DR, Rose JK; , J Biol Chem. 2007;282:12066-12074.: A Tomato Endo-beta-1,4-glucanase, SlCel9C1, Represents a Distinct Subclass with a New Family of Carbohydrate Binding Modules (CBM49). PUBMED:17322304 EPMC:17322304

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR019028

This domain is found at the C-terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose [ PUBMED:17322304 ].

A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and rare instances of independent putative CBMs. The requirement of CBMs existing as modules within larger enzymes sets this class of carbohydrate-binding protein apart from other non-catalytic sugar binding proteins such as lectins and sugar transport proteins.

CBMs were previously classified as cellulose-binding domains (CBDs) based on the initial discovery of several modules that bound cellulose [ PUBMED:3338453 , PUBMED:3134347 ]. However, additional modules in carbohydrate-active enzymes are continually being found that bind carbohydrates other than cellulose yet otherwise meet the CBM criteria, hence the need to reclassify these polypeptides using more inclusive terminology.

Previous classification of cellulose-binding domains were based on amino acid similarity. Groupings of CBDs were called "Types" and numbered with roman numerals (e.g. Type I or Type II CBDs). In keeping with the glycoside hydrolase classification, these groupings are now called families and numbered with Arabic numerals. Families 1 to 13 are the same as Types I to XIII. For a detailed review on the structure and binding modes of CBMs see [ PUBMED:15214846 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan CBD (CL0203), which has the following description:

This superfamily includes several carbohydrate binding domains. These domains have a beta sandwich structure.

The clan contains the following 5 members:

CBM49 CBM_2 CBM_3 CHB_HEX Cohesin


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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Representative proteomes UniProt

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

Representative proteomes UniProt
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_6310 (release 21.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Mistry J , Urbanowicz B
Number in seed: 23
Number in full: 801
Average length of the domain: 82.20 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 16.06 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.4 23.4
Trusted cut-off 23.4 23.4
Noise cut-off 23.3 23.3
Model length: 81
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...


Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0R0H131 View 3D Structure Click here
C0HF28 View 3D Structure Click here
I1K6A1 View 3D Structure Click here
I1KPJ3 View 3D Structure Click here
I1LIS9 View 3D Structure Click here
K7UN70 View 3D Structure Click here
K7URD6 View 3D Structure Click here
P08797 View 3D Structure Click here
P22698 View 3D Structure Click here
Q0J930 View 3D Structure Click here
Q42059 View 3D Structure Click here
Q54BC0 View 3D Structure Click here
Q54BG1 View 3D Structure Click here
Q54CD0 View 3D Structure Click here
Q54CY4 View 3D Structure Click here
Q54DJ1 View 3D Structure Click here
Q54DJ2 View 3D Structure Click here
Q54DJ3 View 3D Structure Click here
Q54DJ4 View 3D Structure Click here
Q54DP5 View 3D Structure Click here
Q54DQ0 View 3D Structure Click here
Q54DQ5 View 3D Structure Click here
Q54DQ7 View 3D Structure Click here
Q54DS7 View 3D Structure Click here
Q54DY8 View 3D Structure Click here
Q54EX0 View 3D Structure Click here
Q54G89 View 3D Structure Click here
Q54HL5 View 3D Structure Click here
Q54JS3 View 3D Structure Click here
Q54JS4 View 3D Structure Click here
Q54LF5 View 3D Structure Click here
Q54LG4 View 3D Structure Click here
Q54LG5 View 3D Structure Click here
Q54PW1 View 3D Structure Click here
Q54S96 View 3D Structure Click here
Q54SS3 View 3D Structure Click here
Q54U76 View 3D Structure Click here
Q54UH2 View 3D Structure Click here
Q54UH3 View 3D Structure Click here
Q54UH4 View 3D Structure Click here

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;