Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.

Uncharacterized conserved protein, DUF1680 family [Function unknown].

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.

Lantibiotic modifying enzyme [Defense mechanisms].

TheGH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482],6EX6_B The GH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482]

Crystalstructure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QJY_B Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]

Glycosidehydrolase BT_1003 [Bacteroides thetaiotaomicron]

Crystalstructure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_B Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_C Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_D Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]