| IED ID | IndEnz0001000365 |
| Enzyme Type ID | amylase000365 |
| Protein Name |
Trehalose synthase EC 5.4.99.16 Maltose alpha-D-glucosyltransferase |
| Gene Name | treS |
| Organism | Pimelobacter sp. (strain R48) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Propionibacteriales Nocardioidaceae Pimelobacter unclassified Pimelobacter Pimelobacter sp. (strain R48) |
| Enzyme Sequence | MSIAESTVLGEEPEWFRTAVFYEVLVRSFRDPNAGGTGDFRGLAEKLDYLQWLGVDCLWVPPFFSSPLRDGGYDVADYTGILPEIGTVEDFHAFLDGAHERGIRVIIDFVMNHTSDAHPWFQASRSDPDGPYGDFYVWSDTDELYQDARVIFVDTEPSNWTWDQTRGQYYWHRFFHHQPDLNFDNPKVQDAMLEAMAFWLDMGLDGFRLDAVPYLYERPGTNGENLPETHEMLKRVRRFVDDNYPDRVLLYEANQWPTDVVEYFGPEEREDGTVVGPESHMAFHFPVMPRIFMAVRRESRFPISEIMEQTPAIPEGCQWGIFLRNHDELTLEMVTDEDRDYMWGEYAKDPRMKANIGIRRRLAPLLDNDTNQIELFTALLLSLPGSPVLYYGDEIGMGDNIWLGDRDGVRTPMQRTPDRNVGFSAATPGKLHLPTIQDPVYGYQSVNVEAQLENPSSLLHWTRRMIHIRRQRDAFGLGTFEDLGGSNPAVLSYVRELPGDGGDDVILCVNNLSRFPQPVELDLRKYEGRVPVELIGGVPFPAVGELPYLLTLSGHGFYWFRLTDPDTTGRPVL |
| Enzyme Length | 573 |
| Uniprot Accession Number | P72235 |
| Absorption | |
| Active Site | ACT_SITE 210; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0R6E0; ACT_SITE 252; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q9ZEU2 |
| Activity Regulation | |
| Binding Site | BINDING 70; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 113; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 178; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 208; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 326; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 327; /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:A0R6E0}; |
| DNA Binding | |
| EC Number | 5.4.99.16 |
| Enzyme Function | FUNCTION: Catalyzes the reversible interconversion of maltose and alpha,alpha-trehalose by transglucosylation. {ECO:0000250|UniProtKB:A0R6E0}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (6); Chain (1); Metal binding (5) |
| Keywords | Calcium;Isomerase;Metal-binding |
| 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 | 65,669 |
| Kinetics | |
| Metal Binding | METAL 112; /note=Calcium; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 180; /note=Calcium; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 214; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 215; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0R6E0; METAL 217; /note=Calcium; /evidence=ECO:0000250|UniProtKB:A0R6E0 |
| Rhea ID | RHEA:15145 |
| Cross Reference Brenda |