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CAZyme Information: MGYG000000032_03208
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Hungatella effluvii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella effluvii | |||||||||||
| CAZyme ID | MGYG000000032_03208 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | Trehalose-6-phosphate hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 99715; End: 101379 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH13 | 25 | 368 | 1e-181 | 0.9941860465116279 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK10933 | PRK10933 | 0.0 | 9 | 554 | 13 | 551 | trehalose-6-phosphate hydrolase; Provisional |
| cd11333 | AmyAc_SI_OligoGlu_DGase | 0.0 | 9 | 466 | 5 | 428 | Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
| TIGR02403 | trehalose_treC | 0.0 | 3 | 553 | 1 | 543 | alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor. |
| COG0366 | AmyA | 1.34e-153 | 9 | 510 | 3 | 490 | Glycosidase [Carbohydrate transport and metabolism]. |
| pfam00128 | Alpha-amylase | 4.77e-147 | 26 | 370 | 1 | 332 | Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SET92238.1 | 3.37e-308 | 1 | 551 | 1 | 546 |
| QRV19974.1 | 2.76e-307 | 1 | 551 | 1 | 546 |
| ADL05887.1 | 2.76e-307 | 1 | 551 | 1 | 546 |
| QHG01163.1 | 3.65e-277 | 1 | 553 | 1 | 549 |
| AXU84096.1 | 4.23e-276 | 1 | 553 | 1 | 549 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5BRQ_A | 9.12e-245 | 4 | 550 | 15 | 561 | Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580] |
| 5BRP_A | 3.69e-244 | 4 | 550 | 15 | 561 | Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580] |
| 1UOK_A | 9.38e-193 | 4 | 550 | 6 | 554 | CrystalStructure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus] |
| 5DO8_A | 1.89e-181 | 4 | 511 | 7 | 516 | 1.8Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_B 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_C 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e] |
| 4M56_A | 3.83e-172 | 4 | 550 | 5 | 557 | TheStructure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],4M56_B The Structure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39795 | 5.65e-239 | 4 | 550 | 9 | 554 | Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2 |
| P28904 | 1.52e-214 | 4 | 516 | 8 | 518 | Trehalose-6-phosphate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=treC PE=1 SV=3 |
| P29094 | 7.33e-198 | 4 | 548 | 6 | 554 | Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1 |
| P21332 | 5.14e-192 | 4 | 550 | 6 | 554 | Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1 |
| Q9K8U9 | 7.48e-190 | 4 | 548 | 6 | 553 | Oligo-1,6-glucosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=malL PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000041 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |