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Links from Protein

Items: 5

1.

Beta-L-arabinofuranosidase, GH127 middle domain

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
Family Accession:
NF044297.2
Method:
HMM
2.

beta-L-arabinofuranosidase domain-containing protein

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
Family Accession:
NF019556.5
Method:
HMM
3.
new record, indexing in progress
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4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
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