| IED ID | IndEnz0001000385 |
| Enzyme Type ID | amylase000385 |
| Protein Name |
Trehalose synthase/amylase TreS EC 3.2.1.1 EC 5.4.99.16 Maltose alpha-D-glucosyltransferase MTase |
| Gene Name | treS MT0134 |
| Organism | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| Enzyme Sequence | MNEAEHSVEHPPVQGSHVEGGVVEHPDAKDFGSAAALPADPTWFKHAVFYEVLVRAFFDASADGSGDLRGLIDRLDYLQWLGIDCIWLPPFYDSPLRDGGYDIRDFYKVLPEFGTVDDFVALVDAAHRRGIRIITDLVMNHTSESHPWFQESRRDPDGPYGDYYVWSDTSERYTDARIIFVDTEESNWSFDPVRRQFYWHRFFSHQPDLNYDNPAVQEAMIDVIRFWLGLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRVRKVVDDEFPGRVLLAEANQWPGDVVEYFGDPNTGGDECHMAFHFPLMPRIFMAVRRESRFPISEIIAQTPPIPDMAQWGIFLRNHDELTLEMVTDEERDYMYAEYAKDPRMKANVGIRRRLAPLLDNDRNQIELFTALLLSLPGSPVLYYGDEIGMGDVIWLGDRDGVRIPMQWTPDRNAGFSTANPGRLYLPPSQDPVYGYQAVNVEAQRDTSTSLLNFTRTMLAVRRRHPAFAVGAFQELGGSNPSVLAYVRQVAGDDGDTVLCVNNLSRFPQPIELDLQQWTNYTPVELTGHVEFPRIGQVPYLLTLPGHGFYWFQLTTHEVGAPPTCGGERRL |
| Enzyme Length | 601 |
| Uniprot Accession Number | P9WQ18 |
| Absorption | |
| Active Site | ACT_SITE 238; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0R6E0; ACT_SITE 280; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q9ZEU2 |
| Activity Regulation | |
| Binding Site | BINDING 98; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 141; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 206; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 236; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 349; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 350; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145, ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16; Evidence={ECO:0000250|UniProtKB:P9WQ19}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P9WQ19}; |
| DNA Binding | |
| EC Number | 3.2.1.1; 5.4.99.16 |
| Enzyme Function | FUNCTION: Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P). Might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS could expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also could expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. {ECO:0000250|UniProtKB:P9WQ19}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000250|UniProtKB:P9WQ19}.; PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis. {ECO:0000250|UniProtKB:P9WQ19}. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (6); Chain (1); Metal binding (5); Region (1) |
| Keywords | Calcium;Capsule biogenesis/degradation;Carbohydrate metabolism;Glycogen biosynthesis;Glycogen metabolism;Glycosidase;Hydrolase;Isomerase;Metal-binding;Polysaccharide degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,593 |
| Kinetics | |
| Metal Binding | METAL 140; /note=Calcium; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 208; /note=Calcium; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 242; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 243; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 245; /note=Calcium; /evidence=ECO:0000250|UniProtKB:A0R6E0 |
| Rhea ID | RHEA:15145 |
| Cross Reference Brenda |