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CAZyme Information: MGYG000001265_03411
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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 | Methylobacterium sp002778835 | |||||||||||
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| Lineage | Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Beijerinckiaceae; Methylobacterium; Methylobacterium sp002778835 | |||||||||||
| CAZyme ID | MGYG000001265_03411 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 28; End: 2418 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| TIGR02457 | TreS_Cterm | 1.96e-134 | 267 | 789 | 3 | 528 | trehalose synthase-fused probable maltokinase. Three pathways for the biosynthesis of trehalose, an osmoprotectant that in some species is also a precursor of certain cell wall glycolipids. Trehalose synthase, TreS, can interconvert maltose and trehalose, but while the equilibrium may favor trehalose, physiological concentrations of trehalose may be much greater than that of maltose and TreS may act largely in its degradation. This model describes a domain found only as a C-terminal fusion to TreS proteins. The most closely related proteins outside this family, Pep2 of Streptomyces coelicolor and Mak1 of Actinoplanes missouriensis, have known maltokinase activity. We suggest this domain acts as a maltokinase and helps drive conversion of trehalose to maltose. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
| cd11334 | AmyAc_TreS | 2.69e-99 | 1 | 163 | 284 | 447 | Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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 (Asp, Glu and Asp) 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. |
| COG3281 | Ble | 1.65e-75 | 404 | 790 | 70 | 430 | Predicted trehalose synthase [Carbohydrate transport and metabolism]. |
| PRK14705 | PRK14705 | 5.04e-51 | 273 | 796 | 5 | 477 | glycogen branching enzyme; Provisional |
| pfam16657 | Malt_amylase_C | 3.56e-32 | 172 | 249 | 1 | 75 | Maltogenic Amylase, C-terminal domain. This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyzes starch material. Maltogenic amylases are central to carbohydrate metabolism. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AWN39287.1 | 0.0 | 1 | 795 | 293 | 1087 |
| AYO81979.1 | 0.0 | 1 | 790 | 293 | 1082 |
| QEE38815.1 | 0.0 | 1 | 794 | 293 | 1086 |
| QGY05841.1 | 0.0 | 1 | 790 | 293 | 1082 |
| ACB23593.1 | 0.0 | 1 | 790 | 293 | 1082 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5H2T_A | 2.32e-109 | 1 | 258 | 309 | 566 | Structureof trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_B Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_C Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_D Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_E Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_F Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_G Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_H Structure of trehalose synthase [Thermomonospora curvata DSM 43183] |
| 5X7U_A | 4.31e-108 | 1 | 252 | 290 | 541 | Trehalosesynthase from Thermobaculum terrenum [Thermobaculum terrenum ATCC BAA-798] |
| 3ZO9_A | 1.38e-103 | 1 | 266 | 322 | 589 | ChainA, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZO9_B Chain B, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZOA_A Chain A, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZOA_B Chain B, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],5JY7_A Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_B Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_C Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_D Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_E Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_F Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_G Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_H Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155] |
| 4LXF_A | 1.10e-102 | 3 | 258 | 351 | 609 | Crystalstructure of M. tuberculosis TreS [Mycobacterium tuberculosis H37Rv],4LXF_B Crystal structure of M. tuberculosis TreS [Mycobacterium tuberculosis H37Rv] |
| 5GTW_A | 5.05e-77 | 1 | 254 | 301 | 555 | TheN253R mutant structures of trehalose synthase from Deinococcus radiodurans display two different active-site conformations [Deinococcus radiodurans R1],5GTW_B The N253R mutant structures of trehalose synthase from Deinococcus radiodurans display two different active-site conformations [Deinococcus radiodurans R1],5GTW_C The N253R mutant structures of trehalose synthase from Deinococcus radiodurans display two different active-site conformations [Deinococcus radiodurans R1],5GTW_D The N253R mutant structures of trehalose synthase from Deinococcus radiodurans display two different active-site conformations [Deinococcus radiodurans R1] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P72235 | 2.55e-106 | 1 | 253 | 307 | 563 | Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1 |
| A0R6E0 | 7.55e-103 | 1 | 266 | 322 | 589 | Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1 |
| P9WQ18 | 3.62e-102 | 3 | 258 | 332 | 590 | Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS PE=3 SV=1 |
| P9WQ19 | 3.62e-102 | 3 | 258 | 332 | 590 | Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treS PE=1 SV=1 |
| O06458 | 7.93e-77 | 1 | 312 | 286 | 609 | Trehalose synthase OS=Thermus thermophilus OX=274 GN=treS 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 |
|---|---|---|---|---|---|
| 1.000073 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |