Species | Odoribacter splanchnicus | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Marinifilaceae; Odoribacter; Odoribacter splanchnicus | |||||||||||
CAZyme ID | MGYG000000254_01813 | |||||||||||
CAZy Family | GH97 | |||||||||||
CAZyme Description | Retaining alpha-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 152363; End: 154303 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH97 | 11 | 644 | 8e-182 | 0.9904912836767037 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam10566 | Glyco_hydro_97 | 1.26e-92 | 298 | 554 | 8 | 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. |
pfam14508 | GH97_N | 3.69e-79 | 27 | 287 | 2 | 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. |
pfam14509 | GH97_C | 1.08e-21 | 557 | 645 | 1 | 95 | 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. |
cd14791 | GH36 | 1.27e-04 | 307 | 407 | 13 | 152 | 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. |
cd14792 | GH27 | 0.001 | 323 | 370 | 32 | 90 | 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 |
---|---|---|---|---|---|
ADY34178.1 | 0.0 | 1 | 646 | 1 | 646 |
SNV44365.1 | 0.0 | 1 | 646 | 1 | 646 |
ABR38697.1 | 0.0 | 1 | 646 | 1 | 647 |
QUT60067.1 | 0.0 | 9 | 646 | 4 | 642 |
QQY40359.1 | 0.0 | 9 | 646 | 4 | 642 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5XFM_A | 0.0 | 20 | 646 | 15 | 642 | 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] |
3A24_A | 1.10e-41 | 25 | 641 | 5 | 635 | Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron] |
5E1Q_A | 1.06e-40 | 25 | 641 | 19 | 649 | 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] |
3WFA_A | 1.77e-36 | 21 | 644 | 2 | 701 | 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] |
2D73_A | 1.87e-36 | 21 | 644 | 22 | 721 | 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 |
---|---|---|---|---|---|---|
D7CFN7 | 9.89e-54 | 26 | 588 | 45 | 564 | Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1 |
Q8A6L0 | 1.62e-41 | 1 | 641 | 1 | 656 | 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 | 7.65e-36 | 1 | 644 | 1 | 721 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000319 | 0.998874 | 0.000259 | 0.000171 | 0.000179 | 0.000174 |
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