| Activities in Family | β-L-arabinofuranosidase (EC 3.2.1.185); |
|---|---|
| Mechanism | Retaining a |
| Clan | GH-P |
| 3D Structure Status | ( α / α ) 6 barrel |
| Catalytic Nucleophile/Base | zinc coordinated cysteine |
| Catalytic Proton Donor | Glu |
| Note | Family created after Luis et al. (2018) Nature Microbiol., [PMID=29255254] who have shown the b-L-arabinofuranosidase activity of BT0349 |
| External resources | CAZypedia; |
| Statistics | GenBank accession (3026); Uniprot accession (3); PDB accession (5); 3D entries (2); cryst (0) |
| Bacteria | |||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | |
| β-L-arabinofuranosidase (BT0349) | 3.2.1.185 | pubmed |
Bacteroides thetaiotaomicron VPI-5482 | AAO75456.1 | A0A6I0SRL5 Q8AAW3 |
5OPJ[A] 6YQH[AAA] 8QF8[A,B] |
|
| β-1,3-L-arabinofuranosidase (Bll3HypBA1; BLLJ_1848) | 3.2.1.185 | doi |
Bifidobacterium longum subsp. longum JCM 1217 | BAJ67512.1 BEG79431.1 |
8K7X[A,A] 8K7Y[A,B] |
||
| β-L-arabinofuranosidase (Bll4HypBA1; BLLJ_0089) | 3.2.1.185 | pubmed |
Bifidobacterium longum subsp. longum JCM 1217 | BAJ65759.1 | |||
| β-1,3-L-arabinofuranosidase (CpAbf127A) | 3.2.1.185 | pubmed |
Caldanaerobius polysaccharolyticus ATCC BAA-17 | WP_026486276.1 | |||
| β-1,2-L-arabinofuranosidase (XeHypBA1; XCV2724; BHE83_06285) | 3.2.1.185 | pubmed |
Xanthomonas euvesicatoria pv. vesicatoria str. 85-10 | AOY66213.1 CAJ24403.1 |
Q3BS08 | ||
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