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].

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only].

Lanthionine synthetase C-like protein. Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains. This region contains seven internal repeats.

ChainAAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482]

Beta-L-arabinofuranosidase[Bacteroides thetaiotaomicron]

Thecrystal structure of native HypBA1 from Bifidobacterium longum JCM 1217 [Bifidobacterium longum subsp. longum JCM 1217],3WRG_A The complex structure of HypBA1 with L-arabinose [Bifidobacterium longum subsp. longum JCM 1217]

Crystalstructure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum ligand free form [Bifidobacterium longum subsp. longum JCM 1217],3WKX_A Crystal structure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum arabinose complex form [Bifidobacterium longum subsp. longum JCM 1217],7BZL_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7DIF_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXV_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXW_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217]

ChainA, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217]

Non-reducing end beta-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA1 PE=1 SV=1