O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].

Glycosyl hydrolase family 30 beta sandwich domain.

Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.

Glycosyl hydrolase family 30 TIM-barrel domain.

Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.

Structureof modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_B Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_C Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_D Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_E Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_F Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_G Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_H Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis]

ChainA, Carbohydrate Binding Family 6 [Acetivibrio thermocellus]

CrystalStructure of XynC from Bacillus subtilis 168 [Bacillus subtilis],3GTN_B Crystal Structure of XynC from Bacillus subtilis 168 [Bacillus subtilis],3KL0_A Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL0_B Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL0_C Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL0_D Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL3_A Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL3_B Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL3_C Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL3_D Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL5_A Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis],3KL5_B Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis],3KL5_C Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis],3KL5_D Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis]

ChainA, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQ9_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQB_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQC_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQD_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQE_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus]

ChainA, xylanase [Dickeya chrysanthemi],2Y24_A Chain A, XYLANASE [Dickeya chrysanthemi]

Glucuronoxylanase XynC OS=Bacillus subtilis (strain 168) OX=224308 GN=xynC PE=1 SV=1

Glucuronoxylanase XynC OS=Bacillus subtilis OX=1423 GN=xynC PE=3 SV=2