| Species | Paraprevotella clara | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella clara | |||||||||||
| CAZyme ID | MGYG000002540_01582 | |||||||||||
| CAZy Family | GH97 | |||||||||||
| CAZyme Description | Glucan 1,4-alpha-glucosidase SusB | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 388424; End: 390352 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH97 | 19 | 636 | 4.8e-167 | 0.9809825673534073 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam14508 | GH97_N | 1.02e-62 | 28 | 296 | 1 | 235 | 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. |
| pfam10566 | Glyco_hydro_97 | 1.93e-62 | 302 | 539 | 1 | 278 | 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. |
| pfam14509 | GH97_C | 2.78e-38 | 542 | 637 | 1 | 97 | 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. |
| cd14792 | GH27 | 2.91e-04 | 311 | 408 | 10 | 122 | glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 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. GH27 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCA49446.1 | 3.38e-297 | 25 | 634 | 28 | 638 |
| QUT42768.1 | 4.05e-297 | 25 | 634 | 33 | 643 |
| QMW87202.1 | 9.65e-297 | 25 | 634 | 28 | 638 |
| AAO75239.1 | 9.65e-297 | 25 | 634 | 28 | 638 |
| ALJ42768.1 | 1.16e-296 | 25 | 634 | 33 | 643 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5E1Q_A | 5.64e-70 | 28 | 637 | 20 | 655 | Mutant(D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482],5E1Q_B Mutant (D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482] |
| 3A24_A | 4.27e-69 | 28 | 637 | 6 | 641 | Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron] |
| 3WFA_A | 1.05e-68 | 25 | 638 | 4 | 705 | 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] |
| 2JKA_A | 1.07e-68 | 25 | 638 | 13 | 714 | 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] |
| 2D73_A | 1.29e-68 | 25 | 638 | 24 | 725 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8A6L0 | 9.50e-70 | 1 | 637 | 1 | 662 | 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 |
| G8JZS4 | 1.38e-68 | 1 | 638 | 1 | 725 | 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 |
| D7CFN7 | 2.83e-45 | 112 | 633 | 95 | 617 | Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.009032 | 0.972326 | 0.017651 | 0.000346 | 0.000319 | 0.000306 |
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