Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; | |||||||||||
CAZyme ID | MGYG000001643_01103 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Isomalto-dextranase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1870; End: 3303 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 205 | 455 | 1.1e-31 | 0.9344978165938864 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17801 | Melibiase_C | 1.34e-15 | 407 | 475 | 6 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
cd14792 | GH27 | 9.20e-08 | 90 | 389 | 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. |
PLN02229 | PLN02229 | 2.56e-07 | 299 | 476 | 240 | 418 | alpha-galactosidase |
PLN02808 | PLN02808 | 1.16e-06 | 277 | 476 | 165 | 384 | alpha-galactosidase |
PLN02692 | PLN02692 | 8.62e-06 | 90 | 472 | 83 | 405 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNT67171.1 | 1.10e-227 | 16 | 475 | 12 | 473 |
QCP71216.1 | 4.54e-196 | 21 | 477 | 18 | 475 |
QCD40129.1 | 4.54e-196 | 21 | 477 | 18 | 475 |
AHF13125.1 | 2.18e-195 | 20 | 477 | 16 | 470 |
QUT44530.1 | 2.35e-195 | 14 | 477 | 12 | 492 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5AWO_A | 1.11e-87 | 54 | 476 | 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 | 1.18e-87 | 54 | 476 | 64 | 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 | 0.000001 | 1.000039 | 0.000000 | 0.000000 | 0.000000 |
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