Species | CAG-873 sp900554265 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900554265 | |||||||||||
CAZyme ID | MGYG000002225_01650 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Isomalto-dextranase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 51; End: 1475 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 195 | 451 | 2.3e-33 | 0.9388646288209607 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17801 | Melibiase_C | 2.54e-18 | 398 | 472 | 1 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
PLN02808 | PLN02808 | 4.76e-12 | 359 | 473 | 261 | 384 | alpha-galactosidase |
PLN02229 | PLN02229 | 9.48e-09 | 375 | 473 | 315 | 418 | alpha-galactosidase |
cd14792 | GH27 | 1.34e-05 | 81 | 385 | 22 | 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. |
PLN02899 | PLN02899 | 1.44e-05 | 390 | 473 | 539 | 631 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNT67171.1 | 2.01e-234 | 11 | 472 | 10 | 473 |
VEH14482.1 | 1.66e-192 | 45 | 474 | 41 | 468 |
QUT44530.1 | 2.28e-192 | 18 | 474 | 19 | 492 |
QUT79686.1 | 2.28e-192 | 18 | 474 | 19 | 492 |
QRM98947.1 | 4.59e-192 | 34 | 474 | 40 | 492 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5AWO_A | 8.69e-90 | 50 | 473 | 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] |
4NX0_A | 1.18e-10 | 191 | 473 | 174 | 441 | Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q44052 | 6.63e-90 | 8 | 473 | 18 | 492 | Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1 |
P14749 | 2.46e-10 | 343 | 473 | 276 | 408 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000635 | 0.159366 | 0.839716 | 0.000089 | 0.000103 | 0.000090 |
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