Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; | |||||||||||
CAZyme ID | MGYG000004599_00124 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Isomalto-dextranase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 53916; End: 55400 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 209 | 471 | 1.1e-34 | 0.9388646288209607 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17801 | Melibiase_C | 4.58e-16 | 420 | 491 | 3 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
PLN02808 | PLN02808 | 1.88e-13 | 302 | 492 | 194 | 384 | alpha-galactosidase |
PLN02229 | PLN02229 | 2.53e-08 | 303 | 492 | 225 | 418 | alpha-galactosidase |
cd14792 | GH27 | 3.36e-08 | 83 | 405 | 11 | 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. |
PLN02692 | PLN02692 | 1.08e-04 | 266 | 488 | 185 | 405 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUU07210.1 | 2.00e-203 | 3 | 493 | 4 | 492 |
QRM98947.1 | 2.00e-203 | 3 | 493 | 4 | 492 |
QUT44530.1 | 8.08e-203 | 3 | 493 | 4 | 492 |
QUT79686.1 | 8.08e-203 | 3 | 493 | 4 | 492 |
QNT67171.1 | 2.10e-186 | 1 | 491 | 1 | 473 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5AWO_A | 9.64e-77 | 55 | 492 | 37 | 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 | 6.05e-15 | 97 | 492 | 49 | 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] |
6F4C_B | 6.44e-07 | 360 | 492 | 228 | 361 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q44052 | 9.83e-77 | 55 | 492 | 63 | 492 | 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 |
---|---|---|---|---|---|
0.000000 | 0.000002 | 1.000062 | 0.000000 | 0.000000 | 0.000000 |
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