| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; | |||||||||||
| CAZyme ID | MGYG000001643_00729 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | Isomalto-dextranase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 9372; End: 10802 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 200 | 454 | 5.2e-31 | 0.9388646288209607 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17801 | Melibiase_C | 3.11e-16 | 406 | 474 | 6 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
| cd14792 | GH27 | 9.60e-08 | 85 | 388 | 28 | 271 | 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 | 5.74e-06 | 378 | 476 | 285 | 385 | alpha-galactosidase |
| PLN02692 | PLN02692 | 9.97e-06 | 379 | 471 | 310 | 405 | alpha-galactosidase |
| PLN02229 | PLN02229 | 1.07e-05 | 378 | 471 | 315 | 414 | alpha-galactosidase |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QCP71216.1 | 2.89e-309 | 1 | 476 | 1 | 475 |
| QCD40129.1 | 2.89e-309 | 1 | 476 | 1 | 475 |
| AHF13125.1 | 1.66e-182 | 3 | 476 | 2 | 470 |
| QUT44530.1 | 1.35e-169 | 3 | 476 | 4 | 492 |
| QUT79686.1 | 1.35e-169 | 3 | 476 | 4 | 492 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AWO_A | 3.42e-66 | 51 | 475 | 38 | 466 | 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 | 1.22e-66 | 51 | 475 | 64 | 492 | Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1 |
| A2R2S6 | 3.13e-07 | 345 | 474 | 266 | 401 | Probable alpha-galactosidase D OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglD PE=3 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000404 | 0.132250 | 0.867124 | 0.000068 | 0.000084 | 0.000074 |
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