| Activities in Family | L-Rhα-α-1,4-GlcA α-L-rhamnohydrolase (EC 3.2.1.-) |
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| Mechanism | Retaining |
| 3D Structure Status | seven-bladed β-propeller |
| Catalytic Nucleophile/Base | His |
| Note | Created 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. |
| External resources | CAZypedia; |
| Statistics | GenBank accession (242); Uniprot accession (1); PDB accession (5); 3D entries (4); cryst (0) |
| Bacteria | ||||||||||||
| Protein Name | EC# | Organism | GenBank | Uniprot |
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| L-Rhα-a-1,4-GlcA α-L-rhamnohydrolase (BACCELL_00856) | 3.2.1.- | Bacteroides cellulosilyticus DSM 14838 | EEF91490.1 |
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| BACINT_00347 | Bacteroides intestinalis DSM 17393 |
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| Bovatus_03783 / BACOVA_03493 | Bacteroides ovatus ATCC 8483 | ALJ48388.1 |
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| 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 |
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