| Activities in Sub Family | α-1,2-L-arabinofuranosidase (EC 3.2.1.-); α-1,3-L-arabinofuranosidase (EC 3.2.1.-); Xylan β-1,4-xylosidase (EC 3.2.1.37); α-L-arabinofuranosidase (EC 3.2.1.55); |
|---|---|
| Mechanism | Inverting e |
| Clan | GH-F |
| 3D Structure Status | 5-fold β-propeller |
| Catalytic Nucleophile/Base | Asp |
| Catalytic Proton Donor | Glu |
| Note | Many members have been assigned to subfamilies as described by Mewis et al. (2016) Appl. Environm. Microbiol. 82:1686-1692 (PMID: 26729713). |
| External resources | CAZypedia; |
| Commercial Enzyme Provider(s) | MEGAZYME; NZYTech; PROZOMIX; |
| Statistics | GenBank accession (201); Uniprot accession (2); |
| Bacteria | ||||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | Subf | |
| α-1,2/1,3-L-arabinofuranosidase (BlArafC; BLLJ_1852) | 3.2.1.- 3.2.1.- |
pubmed pubmed pubmed pubmed |
Bifidobacterium longum subsp. longum JCM 1217 | BAJ67516.1 | 27 | |||
| β-xylosidase / exo-xylanase (GbtXyl43B) (Xyl43B) | 3.2.1.37 | pubmed |
Geobacillus thermoleovorans IT-08 | ABD48561.1 | Q27R94 | 27 | ||
| α-L-arabinofuranosidase (Abf43B) | 3.2.1.55 | pubmed |
Paenibacillus sp. E18 | AFC38437.1 | J9PXM5 | 27 | ||
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