Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.

Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].

Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.

Carbohydrate binding domain. This family includes diverse carbohydrate binding domains.

Glycosyl hydrolase families 32 and 68, which form the clan GH-J. This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

ChainAAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus]

StructureOf An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_B Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_C Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus]

ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus]

ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus]

ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus]

Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1

Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1

Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1

Probable alpha-L-arabinofuranosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abfA PE=3 SV=2

Probable alpha-L-arabinofuranosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=abfA PE=3 SV=2