| IED ID | IndEnz0001000021 |
| Enzyme Type ID | amylase000021 |
| Protein Name |
Trehalose synthase/amylase TreS EC 3.2.1.1 EC 5.4.99.16 Maltose alpha-D-glucosyltransferase MTase |
| Gene Name | treS Rv0126 |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| 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 ATCC 25618 / H37Rv) |
| Enzyme Sequence | MNEAEHSVEHPPVQGSHVEGGVVEHPDAKDFGSAAALPADPTWFKHAVFYEVLVRAFFDASADGSGDLRGLIDRLDYLQWLGIDCIWLPPFYDSPLRDGGYDIRDFYKVLPEFGTVDDFVALVDAAHRRGIRIITDLVMNHTSESHPWFQESRRDPDGPYGDYYVWSDTSERYTDARIIFVDTEESNWSFDPVRRQFYWHRFFSHQPDLNYDNPAVQEAMIDVIRFWLGLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRVRKVVDDEFPGRVLLAEANQWPGDVVEYFGDPNTGGDECHMAFHFPLMPRIFMAVRRESRFPISEIIAQTPPIPDMAQWGIFLRNHDELTLEMVTDEERDYMYAEYAKDPRMKANVGIRRRLAPLLDNDRNQIELFTALLLSLPGSPVLYYGDEIGMGDVIWLGDRDGVRIPMQWTPDRNAGFSTANPGRLYLPPSQDPVYGYQAVNVEAQRDTSTSLLNFTRTMLAVRRRHPAFAVGAFQELGGSNPSVLAYVRQVAGDDGDTVLCVNNLSRFPQPIELDLQQWTNYTPVELTGHVEFPRIGQVPYLLTLPGHGFYWFQLTTHEVGAPPTCGGERRL |
| Enzyme Length | 601 |
| Uniprot Accession Number | P9WQ19 |
| 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:0000269|PubMed:18505459}; 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:0000269|PubMed:18505459}; |
| 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 (PubMed:18505459). 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 (PubMed:18505459). 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) (PubMed:18505459, PubMed:27513637). Might also function as a sensor and/or regulator of trehalose levels within the cell (PubMed:18505459). 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 (PubMed:18505459). {ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:27513637}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:27513637}.; PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis. {ECO:0000269|PubMed:27513637}. |
| 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;Reference proteome |
| 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 | 5.4.99.16; |