Species | Acetatifactor sp900771995 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900771995 | |||||||||||
CAZyme ID | MGYG000002247_00628 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Isomalto-dextranase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 25078; End: 26424 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 171 | 421 | 4.4e-27 | 0.9432314410480349 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17801 | Melibiase_C | 8.65e-11 | 369 | 440 | 3 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
cd14792 | GH27 | 4.47e-07 | 14 | 352 | 8 | 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 | 3.68e-05 | 298 | 442 | 237 | 385 | alpha-galactosidase |
PLN02899 | PLN02899 | 0.002 | 360 | 441 | 540 | 631 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AZB42116.1 | 4.03e-136 | 6 | 445 | 35 | 471 |
QST00336.1 | 3.11e-135 | 4 | 446 | 33 | 472 |
ARI79039.1 | 1.54e-131 | 7 | 446 | 37 | 473 |
AMM31909.1 | 2.33e-124 | 10 | 442 | 60 | 490 |
QQT60490.1 | 2.44e-123 | 10 | 440 | 46 | 457 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5AWO_A | 1.73e-119 | 10 | 442 | 37 | 467 | 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 | 4.67e-13 | 8 | 442 | 23 | 442 | 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 | 2.03e-119 | 10 | 442 | 63 | 493 | Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000045 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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