| Activities in Family | α-L-fucosidase (EC 3.2.1.51); Endo-β-1,4-xylanase (EC 3.2.1.8); |
|---|---|
| Mechanism | Unknown e |
| 3D Structure Status | parallel β-helix |
| Catalytic Nucleophile/Base | Asp |
| Catalytic Proton Donor | Asp |
| Note | Created after Ndeh et al., Nature (2017) 544:65-70 (PMID=28329766) who have shown the a-L-fucosidase activity of the B. thetaiotaomicron enzyme. The xylanase activity of the (Rumini)clostridium thermocellum enzyme was shown by Heinze et al. (PMID=28894250) |
| External resources | CAZypedia; |
| Statistics | GenBank accession (1308); Uniprot accession (2); PDB accession (1); 3D entries (1); cryst (0) |
| Bacteria | |||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | |
| xylanase E (XynE; Cthe_2195) (Xyn141E) | 3.2.1.8 | pubmed |
Acetivibrio thermocellus ATCC 27405 | ABN53397.1 | A3DHG8 | ||
| α-L-fucosidase (BT1002;BT_1002) (specific to α-3-[2-O-methyl]xylose-modified fucose in RG-II chain F) | 3.2.1.51 | pubmed |
Bacteroides thetaiotaomicron VPI-5482 | AAO76109.1 | Q8A915 | 5MQP[A,B,C,D,E,F,G,H] | |
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