Glycoside Hydrolase Family 145

Activities in FamilyL-Rhα-α-1,4-GlcA-specific α-L-rhamnosidase (EC 3.2.1.-)
Mechanism Retaining
3D Structure Statusseven-bladed β-propeller
Catalytic Nucleophile/BaseHis
NoteCreated after Munoz-Munoz et al., Proc. Natl. Acad. Sci. USA (2017) (PMID=28396425); these enzymes hydrolyze a-L-rhamnose residues linked to position 4 of a glucuronic acid using an unusual catalytic machinery comprising a histidine residue. The active site of these a-L-rhamnosidases is located on the opposite side of CAZymes with similar b-propeller folds. Surprisingly, the "normal" side of the b-propeller bears the highest residue conservation in the family and may well have another function. The latter is unknown but strong ressemblance to family PL25 suggests a polysaccharide lyase activity.
Statistics GenBank accession (94); Uniprot accession (1); PDB accession (5); 3D entries (4); cryst (0)
Bacteria
Protein Name EC#OrganismGenBankUniprot
PDB/3D Carbohydrate Ligands Resolution (Å)
 L-Rhα-a-1,4-GlcA α-L-rhamnohydrolase (BACCELL_00856) 3.2.1.- Bacteroides cellulosilyticus DSM 14838 EEF91490.1  
5MVH[A] 1.80
 BACINT_00347   Bacteroides intestinalis DSM 17393    
5MUM[A] 1.80
 Bovatus_03783 / BACOVA_03493   Bacteroides ovatus ATCC 8483 ALJ48388.1  
4IRT[A] 1.74
 L-Rhα-a-1,4-GlcA α-L-rhamnohydrolase / exo-acting α-L-rhamnosidase (BT3686;BT_3686) 3.2.1.- Bacteroides thetaiotaomicron VPI-5482 AAO78791.1  
5MUK[A] 1.49
5MUL[A] β-D-GlcpA
1.39
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