| Species | UMGS1783 sp900555065 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; UMGS1783; UMGS1783; UMGS1783 sp900555065 | |||||||||||
| CAZyme ID | MGYG000004089_01095 | |||||||||||
| CAZy Family | GH36 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 31368; End: 33389 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH36 | 38 | 479 | 7.7e-56 | 0.6133720930232558 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14791 | GH36 | 1.18e-35 | 273 | 574 | 17 | 294 | 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. |
| pfam02065 | Melibiase | 9.08e-29 | 239 | 473 | 25 | 247 | Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27. |
| COG3345 | GalA | 3.58e-17 | 189 | 479 | 230 | 498 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
| cd14792 | GH27 | 3.24e-06 | 261 | 343 | 7 | 82 | 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBO33698.1 | 5.30e-129 | 27 | 655 | 47 | 669 |
| QOY88337.1 | 4.49e-128 | 28 | 673 | 171 | 791 |
| BBO31825.1 | 1.16e-126 | 27 | 672 | 45 | 684 |
| BBO33728.1 | 1.32e-124 | 27 | 655 | 46 | 668 |
| BBO33735.1 | 1.63e-112 | 12 | 671 | 44 | 687 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3MI6_A | 2.83e-21 | 210 | 473 | 285 | 536 | ChainA, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_B Chain B, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_C Chain C, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_D Chain D, Alpha-galactosidase [Levilactobacillus brevis ATCC 367] |
| 2XN0_A | 3.42e-20 | 210 | 473 | 288 | 539 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM] |
| 2XN2_A | 7.88e-20 | 210 | 473 | 288 | 539 | Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM] |
| 6JHP_A | 3.29e-19 | 116 | 476 | 235 | 571 | Crystalstructure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_B Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_C Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_D Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'] |
| 6PHU_A | 2.52e-16 | 210 | 477 | 298 | 552 | SpAgawild type apo structure [Streptococcus pneumoniae TIGR4],6PHV_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P16551 | 2.88e-22 | 157 | 479 | 186 | 498 | Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1 |
| Q92457 | 5.07e-21 | 110 | 477 | 216 | 557 | Alpha-galactosidase 2 OS=Hypocrea jecorina OX=51453 GN=agl2 PE=1 SV=1 |
| P43469 | 1.12e-20 | 142 | 476 | 208 | 532 | Alpha-galactosidase 2 OS=Pediococcus pentosaceus OX=1255 GN=agaS PE=3 SV=1 |
| Q2TW69 | 6.31e-20 | 16 | 476 | 113 | 562 | Probable alpha-galactosidase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglC PE=3 SV=1 |
| B8NWY6 | 6.31e-20 | 16 | 476 | 113 | 562 | Probable alpha-galactosidase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglC PE=3 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000081 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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