| Activities in Sub Family | α-1,3-L-arabinofuranosidase (EC 3.2.1.-); Exo-α-1,5-L-arabinofuranosidase (EC 3.2.1.-); Xylan β-1,4-xylosidase (EC 3.2.1.37); α-L-arabinofuranosidase (EC 3.2.1.55); [inverting] endo-α-1,5-L-arabinanase (EC 3.2.1.99); |
|---|---|
| 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 (323); Uniprot accession (3); |
| Bacteria | ||||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | Subf | |
| β-xylosidase (BAD_1527; BAD1527) | 3.2.1.37 | pubmed |
Bifidobacterium adolescentis ATCC 15703 | BAF40308.1 | A1A3M5 | 22 | ||
| bimodular α-1,3- and α-1,4-L-arabinofuranosidase (BlArafE; BLLJ_1850) | 3.2.1.- | pubmed |
Bifidobacterium longum subsp. longum JCM 1217 | BAJ67514.1 | 22 | |||
| bimodular α-1,5- and α-1,2-arabinofuranosidase (BlArafD; BLLJ_1851) | 3.2.1.99 | pubmed |
Bifidobacterium longum subsp. longum JCM 1217 | BAJ67515.1 | 22 | |||
| exo-α-1,5-L-arabinofuranosidase (BlArafB; BLLJ_1853) | 3.2.1.- | pubmed |
Bifidobacterium longum subsp. longum JCM 1217 | BAJ67517.1 | 22 | |||
| α-1,3-L-arabinofuranosidase (BlArafA; BLLJ_1854) | 3.2.1.- | pubmed |
Bifidobacterium longum subsp. longum JCM 1217 | BAJ67518.1 | A0A3R0A696 | 22 | ||
| arabinanase 43A (RjAbn43A) (Abn43A) | 3.2.1.55 | pubmed |
Ruminiclostridium josui JCM 17888 | BBA94052.1 | A0A2Z5U6M1 | 22 | ||
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