Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; | |||||||||||
CAZyme ID | MGYG000002717_01776 | |||||||||||
CAZy Family | GH97 | |||||||||||
CAZyme Description | Retaining alpha-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 5703; End: 7682 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH97 | 13 | 656 | 2.4e-197 | 0.9952456418383518 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam10566 | Glyco_hydro_97 | 1.33e-123 | 284 | 559 | 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. |
pfam14508 | GH97_N | 5.06e-81 | 29 | 279 | 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. |
pfam14509 | GH97_C | 1.79e-36 | 562 | 657 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBK86458.1 | 0.0 | 4 | 659 | 13 | 668 |
QUT61529.1 | 0.0 | 4 | 659 | 5 | 660 |
QQA30035.1 | 0.0 | 4 | 659 | 5 | 660 |
QUT37383.1 | 0.0 | 4 | 659 | 5 | 660 |
QPH58760.1 | 0.0 | 4 | 659 | 2 | 657 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3A24_A | 6.82e-102 | 29 | 656 | 6 | 640 | Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron] |
5E1Q_A | 1.05e-100 | 29 | 656 | 20 | 654 | 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] |
5HQ4_A | 8.17e-94 | 26 | 659 | 2 | 661 | AGlycoside Hydrolase Family 97 enzyme from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8],5HQA_A A Glycoside Hydrolase Family 97 enzyme in complex with Acarbose from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8] |
5HQC_A | 8.17e-94 | 26 | 659 | 2 | 661 | AGlycoside Hydrolase Family 97 enzyme R171K variant from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8] |
5HQB_A | 2.24e-93 | 26 | 659 | 2 | 661 | AGlycoside Hydrolase Family 97 enzyme (E480Q) in complex with Panose from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8A6L0 | 1.25e-105 | 4 | 656 | 2 | 661 | 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 | 2.04e-69 | 4 | 659 | 2 | 726 | 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 | 7.76e-66 | 8 | 651 | 17 | 615 | 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 |
---|---|---|---|---|---|
0.000347 | 0.998877 | 0.000249 | 0.000167 | 0.000169 | 0.000166 |
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