| Species | Bacteroides graminisolvens | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides graminisolvens | |||||||||||
| CAZyme ID | MGYG000003064_00170 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | Isomalto-dextranase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 246944; End: 248263 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 175 | 417 | 3.4e-31 | 0.9388646288209607 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17801 | Melibiase_C | 5.91e-16 | 366 | 437 | 7 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
| cd14792 | GH27 | 7.46e-12 | 33 | 345 | 2 | 269 | 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. |
| PLN02808 | PLN02808 | 1.32e-09 | 304 | 434 | 251 | 380 | alpha-galactosidase |
| PLN02229 | PLN02229 | 6.90e-07 | 304 | 434 | 281 | 414 | alpha-galactosidase |
| cd14791 | GH36 | 9.87e-06 | 36 | 246 | 6 | 220 | 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUT92727.1 | 4.52e-212 | 21 | 438 | 24 | 442 |
| ALJ61711.1 | 3.69e-211 | 21 | 438 | 24 | 442 |
| QUR46778.1 | 8.78e-170 | 72 | 437 | 1 | 366 |
| QDM09865.1 | 2.79e-165 | 2 | 438 | 4 | 444 |
| QUT79841.1 | 1.61e-164 | 19 | 438 | 11 | 434 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AWO_A | 3.95e-133 | 17 | 437 | 22 | 465 | Arthrobacterglobiformis T6 isomalto-dextranse [Arthrobacter globiformis],5AWP_A Arthrobacter globiformis T6 isomalto-dextranase complexed with isomaltose [Arthrobacter globiformis],5AWQ_A Arthrobacter globiformis T6 isomalto-dextranse complexed with panose [Arthrobacter globiformis] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q44052 | 4.78e-133 | 17 | 437 | 48 | 491 | Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1 |
| Q8RX86 | 3.55e-11 | 106 | 439 | 111 | 393 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000201 | 0.999209 | 0.000153 | 0.000151 | 0.000133 | 0.000127 |
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