Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.

Glycosyl-hydrolase 97 N-terminal. This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.

Glycosyl-hydrolase 97 C-terminal, oligomerization. Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.

glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

Crystalstructure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_B Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_C Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_D Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron]

Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron]

Catalyticrole of the calcium ion in GH97 inverting glycoside hydrolase [Bacteroides thetaiotaomicron],3WFA_B Catalytic role of the calcium ion in GH97 inverting glycoside hydrolase [Bacteroides thetaiotaomicron]

Nativestructure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JKA_B Native structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JKE_A Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with deoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],2JKE_B Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with deoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],2JKP_A Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine [Bacteroides thetaiotaomicron VPI-5482],2JKP_B Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine [Bacteroides thetaiotaomicron VPI-5482]

CrystalStructure Analysis of SusB [Bacteroides thetaiotaomicron VPI-5482],2D73_B Crystal Structure Analysis of SusB [Bacteroides thetaiotaomicron VPI-5482],2ZQ0_A Crystal structure of SusB complexed with acarbose [Bacteroides thetaiotaomicron],2ZQ0_B Crystal structure of SusB complexed with acarbose [Bacteroides thetaiotaomicron]

Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1

Retaining alpha-galactosidase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1871 PE=1 SV=1

Glucan 1,4-alpha-glucosidase SusB OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=susB PE=1 SV=1