Species | CAG-485 sp900759795 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900759795 | |||||||||||
CAZyme ID | MGYG000004208_01505 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Isomalto-dextranase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 15859; End: 17274 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 177 | 449 | 9.7e-31 | 0.9388646288209607 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17801 | Melibiase_C | 3.99e-16 | 398 | 469 | 3 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
PLN02229 | PLN02229 | 9.60e-07 | 360 | 470 | 302 | 418 | alpha-galactosidase |
cd14792 | GH27 | 1.37e-06 | 88 | 383 | 32 | 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. |
cd14791 | GH36 | 8.49e-05 | 121 | 278 | 67 | 217 | glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 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. GH36 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 | 2.69e-04 | 301 | 470 | 212 | 384 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNT67171.1 | 5.95e-202 | 36 | 469 | 37 | 473 |
QUU07210.1 | 4.80e-186 | 39 | 471 | 50 | 492 |
VEH14482.1 | 4.98e-186 | 43 | 471 | 41 | 468 |
QUT44530.1 | 1.94e-185 | 39 | 471 | 50 | 492 |
QUT79686.1 | 1.94e-185 | 39 | 471 | 50 | 492 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5AWO_A | 1.23e-92 | 48 | 470 | 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 | 1.33e-92 | 48 | 470 | 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 |
---|---|---|---|---|---|
0.000015 | 0.010687 | 0.989328 | 0.000004 | 0.000006 | 0.000004 |
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