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Items: 9

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.

DUF4986 domain-containing protein

This domain is found in Rhamnogalacturonan lyase from Bacteroides thetaiotaomicron (Swiss:Q8AAW3) and other bacterial proteins. It shows an alpha/beta structure [1] and locates C-terminal to Pfam:PF07944. The specific function of this domain is still unknown. [1]. 29255254. Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, Basle A, Cartmell A, Terrapon N, Stott K, Lowe EC, McLean R, Shearer K, Schuckel J, Venditto I, Ralet MC, Henrissat B, Martens EC, Mosimann SC, Abbott DW, Gilbert HJ;. Nat Microbiol. 2018;3:210-219. (from Pfam)

Date:
2024-10-16
Family Accession:
NF027693.5
Method:
HMM
3.

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
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.

glycoside hydrolase family 127 protein

glycoside hydrolase family 127 protein similar to Bifidobacterium longum beta-L-arabinofuranosidase that releases L-arabinose from the L-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration; contains a DUF4986 domain

Date:
2020-12-07
Family Accession:
11172113
Method:
Sparcle
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