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 (534); Uniprot accession (5); PDB accession (2); 3D entries (2); cryst (0) |
Bacteria | ||||||||||
Protein Name | EC# | Organism | GenBank | Uniprot |
| Subf | ||||
α-L-arabinofuranosidase (BT3675; BT_3675) | 3.2.1.55 | Bacteroides thetaiotaomicron VPI-5482 | AAO78780.1 NP_812586.1 |
Q8A1I6 |
|
34 | ||||
[grape RGII] α-L-arabinofuranosidase 43F (cleaves L-Araf-α-1,3-D-GalA) (BtAbf43F; BT3662; BT_3662) (Abf43F) | 3.2.1.55 | Bacteroides thetaiotaomicron VPI-5482 | AAO78767.1 NP_812573.1 |
Q8A1J9 |
|
34 | ||||
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