Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.

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

Predicted alpha-1,6-mannanase, GH76 family [Carbohydrate transport and metabolism].

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.

Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.

Crystalstructure of a putative glycosylhydrolase (BT_3782) from Bacteroides thetaiotaomicron VPI-5482 at 1.89 A resolution [Bacteroides thetaiotaomicron VPI-5482],4MU9_B Crystal structure of a putative glycosylhydrolase (BT_3782) from Bacteroides thetaiotaomicron VPI-5482 at 1.89 A resolution [Bacteroides thetaiotaomicron VPI-5482]

Glycosidehydrolase family 76 (mannosidase) Bt3792 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],4C1S_B Glycoside hydrolase family 76 (mannosidase) Bt3792 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482]

CrystalStructure of a family 76 glycoside hydrolase from a bovine Bacteroides thetaiotaomicron strain [Bacteroides thetaiotaomicron]

Structureof the GH76 alpha-mannanase BT2949 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],4V1S_B Structure of the GH76 alpha-mannanase BT2949 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Structureof the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6],6SHD_B Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6],6SHD_C Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6]