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CAZyme Information: MGYG000000923_00780
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Phocaeicola sp900552645 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900552645 | |||||||||||
| CAZyme ID | MGYG000000923_00780 | |||||||||||
| CAZy Family | GH97 | |||||||||||
| CAZyme Description | Retaining alpha-galactosidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 224929; End: 226875 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH97 | 12 | 645 | 2.5e-177 | 0.9889064976228209 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam10566 | Glyco_hydro_97 | 1.72e-88 | 297 | 555 | 6 | 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 | 1.00e-70 | 26 | 288 | 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 | 5.80e-20 | 558 | 645 | 1 | 94 | 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. |
| cd11573 | GH99_GH71_like | 0.003 | 383 | 453 | 7 | 81 | Glycoside hydrolase families 71, 99, and related domains. This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ABR38697.1 | 0.0 | 1 | 647 | 1 | 647 |
| QEW34830.1 | 0.0 | 7 | 647 | 2 | 642 |
| QQY40359.1 | 0.0 | 7 | 647 | 2 | 642 |
| QQY44785.1 | 0.0 | 7 | 647 | 2 | 642 |
| QJR79277.1 | 0.0 | 7 | 647 | 2 | 642 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5XFM_A | 0.0 | 20 | 644 | 15 | 639 | 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 | 1.74e-46 | 26 | 645 | 6 | 638 | Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron] |
| 5E1Q_A | 1.79e-45 | 26 | 645 | 20 | 652 | 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 | 3.37e-35 | 24 | 610 | 5 | 657 | 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 | 3.39e-35 | 24 | 610 | 14 | 666 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8A6L0 | 9.48e-49 | 1 | 645 | 1 | 659 | 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 |
| D7CFN7 | 1.25e-48 | 25 | 586 | 44 | 561 | Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1 |
| G8JZS4 | 1.05e-35 | 1 | 610 | 1 | 677 | 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 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000437 | 0.998532 | 0.000441 | 0.000197 | 0.000186 | 0.000181 |