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 (327); Uniprot accession (10); PDB accession (5); 3D entries (3); cryst (0)

Bacteria
Protein Name	EC#	Organism	GenBank	Uniprot	PDB/3D Carbohydrate Ligands Resolution (Å)	Subf
α-L-arabinofuranosidase (Xsa43E;bpr_I2319)	3.2.1.37 3.2.1.55	Butyrivibrio proteoclasticus B316	ADL35052.1	E0RYY0	4NOV[A] 1.33	29
α-1,2-L-arabinofuranosidase 43A (CJA_3018) (arabinan-specific) (Abf43A=Gly43N)	3.2.1.-	Cellvibrio japonicus Ueda107	ACE83886.1	B3PD60	3QED[A,B,C,D] 2.99 3QEE[A,B] 1.64 3QEF[A,B] α-L-Araf-(1-5)-α-L-Araf-(1-5)-α-L-Araf α-L-Araf-(1-5)[α-L-Araf-(1-3)]-α-L-Araf-(1-5)-α-L-Araf 1.79	29
Pedsa_2569		Pseudopedobacter saltans DSM 12145	ADY53113.1		8HCJ[A,B,C,D,E,F,G,H] 2.57	29
Top

Last update: 2024-07-09 © Copyright 1998-2024
AFMB - CNRS - Université d'Aix-Marseille