DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.

Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.

DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.

Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism].

ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],1GKL_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],1WB4_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB4_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB5_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB5_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1WB6_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],1WB6_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus]

ChainA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus]

ChainA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1GKK_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],3ZI7_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus YS],3ZI7_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus YS],4BAG_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],4BAG_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],4H35_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],4H35_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],5FXM_A Chain A, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],6Y8G_AAA Chain AAA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],6Y8G_BBB Chain BBB, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus]

ChainAAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWO_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWP_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWQ_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B]

Family9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Cellobiose [Thermotoga maritima],1I8A_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Glucose [Thermotoga maritima],1I8U_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a [Thermotoga maritima]

Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1

Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1

Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1

Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1