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 (1351); Uniprot accession (17); PDB accession (8); 3D entries (4); cryst (0) |
Bacteria | ||||||||||||||||||
Protein Name | EC# | Organism | GenBank | Uniprot |
| Subf | ||||||||||||
β-xylosidase (Abf2;CAC1529) | Clostridium acetobutylicum ATCC 824 | AAK79496.1 NP_348156.1 |
|
26 | ||||||||||||||
α-L-arabinofuranosidase II (Araf43;LbAraf43;N624_1993) | 3.2.1.- | Levilactobacillus brevis DSM 1269 / TMW 1.313 | APU52333.1 KIO95879.1 |
A0A5B7Y0Z3 |
|
26 | ||||||||||||
exo-α-1,5-L-arabinofuranosidase 43A (SaAraf43A; SAV1043) (Araf43A) | 3.2.1.- | Streptomyces avermitilis MA-4680 = NBRC 14893 | BAC68753.1 NP_822218.1 |
Q82P90 |
|
26 | ||||||||||||
α-L-arabinofuranosidase (Araf43;WAraf43) | 3.2.1.- | Weissella sp. 142 | APU52332.1 | A0A0D1M7L2 A0A1L7HA00 |
|
26 | ||||||||||||
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