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CAZyme Information: MGYG000000043_00568
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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 sp900066455 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900066455 | |||||||||||
| CAZyme ID | MGYG000000043_00568 | |||||||||||
| CAZy Family | GH97 | |||||||||||
| CAZyme Description | Retaining alpha-galactosidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 100016; End: 101956 Strand: + | |||||||||||
Full Sequence Download help
| MKKQVLFGTL ALLASQAFAQ QAAVTGPDAR LKLDFQLQDG KPVYSVTYDG KTVLENSPLG | 60 |
| FVSNIGDFSR QMTFVDQQTD KVDKTYTQTR IKRSTVHYAA NKLTVTLENA DKKKVDIVFQ | 120 |
| LSNNDIAFRY EMPQYGETAC MVVEKEATGF DFPSSTTTFL SPQSDPMIGW MRTKPSYEEE | 180 |
| YVPDEPVATP SKYGEGYTFP ALFHVGDNWA LVSETGVRSL YCASHLSDAT KDGLYSIAFP | 240 |
| NPGEMNGLGS STPGLALPGV TPWRTITVGN GLKPIVETTV PFDVVDPLYE PSQDYKFGRS | 300 |
| TWSWIMWQDP SINYDDQVRF IDLASEMGYE YTLIDGGWEK NIGRDKMEKL FQYAHQKKVD | 360 |
| VFVWYNSNGY WNDAPQDAKQ CMSNSVARKK EMKWLQKCGV KGLKVDFFGS DKQQMMGLYE | 420 |
| DILTDANEYG LMIIFHGCTI PRGWERMYPN YVGSEAVLAS ENLIFNQHFD DMEAYNACLH | 480 |
| PFIRNTIGCM EFGGTLLNKR YNRTNDGGCT RKTTDVFQLA TAVLYQNPLQ NFALAPNNLT | 540 |
| DAPALAIDFM KQVPTTWDET VFLDGYPGKY CVLARRHGDR WYVVGVNAQK EPLKLTLNLP | 600 |
| MWQKGETVSY YLDDKKRQPK LEDLKIKNPS EVKVVIQPEG GIVLTK | 646 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH97 | 12 | 644 | 4.1e-173 | 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 | 3.28e-93 | 296 | 554 | 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 | 2.25e-72 | 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 | 2.49e-18 | 557 | 644 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ADY36919.1 | 0.0 | 1 | 646 | 1 | 647 |
| ABR38697.1 | 0.0 | 1 | 646 | 1 | 647 |
| QJR70612.1 | 0.0 | 10 | 646 | 5 | 642 |
| AND19139.1 | 0.0 | 10 | 646 | 5 | 642 |
| QJR74675.1 | 0.0 | 10 | 646 | 5 | 642 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5XFM_A | 2.76e-305 | 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 | 2.60e-39 | 27 | 644 | 7 | 638 | Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron] |
| 5E1Q_A | 2.40e-38 | 27 | 644 | 21 | 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 | 8.24e-30 | 21 | 645 | 2 | 702 | 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 | 8.51e-30 | 21 | 645 | 22 | 722 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D7CFN7 | 1.74e-52 | 22 | 588 | 41 | 564 | Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1 |
| Q8A6L0 | 2.79e-39 | 9 | 644 | 14 | 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 |
| G8JZS4 | 3.54e-30 | 1 | 645 | 1 | 722 | 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 |
|---|---|---|---|---|---|
| 0.000352 | 0.998787 | 0.000239 | 0.000209 | 0.000201 | 0.000189 |