Protein Family Models

This entry represents the second beta sandwich domain found in enzymes belonging to the glycosyl hydrolase 127 family [1]. The beta-sandwich domain is somewhat similar to the N-terminal domain of ErbB4 kinase and is involved in formation of a dimer, which is created by a crystallographic 2-fold axis [1]. Paper describing PDB structure 3wkw. [1]. 24680821. Crystal structure of glycoside hydrolase family 127 beta-l-arabinofuranosidase from Bifidobacterium longum. Ito T, Saikawa K, Kim S, Fujita K, Ishiwata A, Kaeothip S, Arakawa T, Wakagi T, Beckham GT, Ito Y, Fushinobu S;. Biochem Biophys Res Commun. 2014;447:32-37. Paper describing PDB structure 5mqo. [2]. 28329766. Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Ndeh D, Rogowski A, Cartmell A, Luis AS, Basle A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, Gilbert HJ;. Nature. 2017;544:65-70. (from Pfam)

Date:

2024-10-16

This entry represents the first of two beta sandwich domains found in the beta-L-arabinofuranosidase enzyme, EC:3.2.1.185 [1]. This domain shows a similarity to C-terminal domains of GH44, GH27, and GH39 enzymes [1]. [1]. 24385433. Characterization of a novel beta-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member. Fujita K, Takashi Y, Obuchi E, Kitahara K, Suganuma T;. J Biol Chem. 2014;289:5240-5249. (from Pfam)

Date:

2024-10-16

This entry represents the catalytic domain of Non-reducing end beta-L-arabinofuranosidase from Bifidobacterium longum (Beta -AFase) and similar proteins that belong to the glycoside hydrolase family 127 (GH127). This domain folds into an (alpha /alpha)6 barrel. Beta-AFase has been characterised as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It releases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration [1,2]. [1]. 24385433. Characterization of a novel beta-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member. Fujita K, Takashi Y, Obuchi E, Kitahara K, Suganuma T;. J Biol Chem. 2014;289:5240-5249. [2]. 24680821. Crystal structure of glycoside hydrolase family 127 beta-l-arabinofuranosidase from Bifidobacterium longum. Ito T, Saikawa K, Kim S, Fujita K, Ishiwata A, Kaeothip S, Arakawa T, Wakagi T, Beckham GT, Ito Y, Fushinobu S;. Biochem Biophys Res Commun. 2014;447:32-37. (from Pfam)

Date:

2024-10-16

glycoside hydrolase 127 (GH127) family protein which may be a beta-L-arabinofuranosidase and release L-arabinose from the non-reducing end of various substrates such as L-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylate 1-alkanols with retention of the anomeric configuration; similar to Geobacillus stearothermophilus GH127 beta-L-arabinofuranosidase Ara127N

Date:

2021-01-25