Carbohydrate-Binding Module Family 40

Known ActivitiesModules of approx. 200 residues, found at the N-terminus of GH33 sialidases. Can also be found inserted in the β-propeller of GH33 sialidases. The sialic acid binding function has been demonstrated for the N-terminal CBM40 of Vibrio cholerae sialidase (Moustafa et al. (2004) J Biol Chem 279:40819-26) (PMID: 15226294).
3D Structure Statuslectin-like
External resourcesHOMSTRAD; InterPro; PFAM;
Statistics GenBank accession (110); Uniprot accession (52); PDB accession (14); 3D entries (4); cryst (0)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 exo-α-sialidase (NanH) 3.2.1.18 Clostridium perfringens A99 CAA60796.1 Q59310  
 exo-α-sialidase (NanJ;CPE0553) 3.2.1.18 Clostridium perfringens str. 13 BAB80259.1
NP_561469.1
Q8XMY5 2V73[A,B]
 exo-α-sialidase (NanI;CPE0725) 3.2.1.18 Clostridium perfringens str. 13 BAB80431.1
NP_561641.1
Q8XMG4  
 sialidase (NanH;SiaH) 3.2.1.18 Clostridium tertium CAA69951.1 P77848  
 sialidase (NanH) 3.2.1.18 Erysipelothrix rhusiopathiae FUJISAWA BAB40435.1 Q9AJR8  
 sialidase A (NanA) 3.2.1.18 Streptococcus pneumoniae 6 ACJ76903.1
CAA51473.1
B8XTT3
P62575
Q59959
 
 sialidase B (NanB) 3.2.1.18 Streptococcus pneumoniae 6 AAC44396.1
AAW08718.1
Q54727  
 (trans-)sialidase B (NanB;SP1687) 2.4.1.-
3.2.1.18
Streptococcus pneumoniae TIGR4 AAK75766.1
NP_346126.1
  2JKB[A]
2VW0[A]
2VW1[A]
2VW2[A]
 sialidase (NanH) 3.2.1.18 Vibrio cholerae 569B 395 AAA27546.1
AAA27547.1
P37060.1 1KIT[A]
1W0O[A]
1W0P[A]
2W68[A,B,C]
 sialidase (NanH) 3.2.1.18 Vibrio cholerae 569B 395 AAA27546.1 P37060.1 1KIT[A]
1W0O[A]
1W0P[A]
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 sialidase L 3.2.1.18 Macrobdella decora AAC47263.1 Q27701 1SLI[A]
1SLL[A]
2SLI[A]
3SLI[A]
4SLI[A]

Footnotes

Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.