| IED ID | IndEnz0001000390 |
| Enzyme Type ID | amylase000390 |
| Protein Name |
Trehalose-6-phosphate hydrolase EC 3.2.1.93 Alpha,alpha-phosphotrehalase Phospho-alpha- 1-1 -glucosidase |
| Gene Name | treA treC BSU07810 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MKTEQTPWWKKAVVYQIYPKSFNDTTGNGVGDLNGIIEKLDYLKTLQVDVLWLTPIYDSPQHDNGYDIRDYYSIYPEYGTMEDFERLVSEAHKRDLKVVMDLVVNHTSTEHKWFREAISSIDSPYRDFYIWKKPQENGSVPTNWESKFGGSAWELDEASGQYYLHLFDVTQADLNWENEEVRKHVYDMMHFWFEKGIDGFRLDVINLISKDQRFPNAEEGDGRSFYTDGPRVHEFLHEMNEKVFSHYDSMTVGEMSSTTVDHCIRYTNPDNKELDMTFSFHHLKVDYPNGEKWALAPFDFLKLKEILSDWQTGMHAGGGWNALFWCNHDQPRVVSRYGDDGAYRVKSAKMLATAIHMMQGTPYIYQGEELGMTNPKFTDISSYRDVESLNMYHAFKEKGMADQDITAILQAKSRDNSRTPVQWDATENGGFTTGTPWIPVAGNYREINAEAALRDQNSVFYHYQKLIQIRKMYDIVTEGTYEIIAKDDPNIFAYLRHGSNEKLLVINNFYGTEAAFTLPDSLAPDEWKAEVLLTNDEAREGLQNMTLRPYESIVYRLTKPC |
| Enzyme Length | 561 |
| Uniprot Accession Number | P39795 |
| Absorption | |
| Active Site | ACT_SITE 203; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00691; ACT_SITE 254; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P00691 |
| Activity Regulation | ACTIVITY REGULATION: Activity is stimulated by high salt concentrations with different efficiencies depending on the kind of salt. In vitro, inhibited by glucose. {ECO:0000269|PubMed:7751281}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-glucose 6-phosphate; Xref=Rhea:RHEA:23008, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:58429, ChEBI:CHEBI:61548; EC=3.2.1.93; Evidence={ECO:0000269|PubMed:7651129, ECO:0000269|PubMed:7751281}; |
| DNA Binding | |
| EC Number | 3.2.1.93 |
| Enzyme Function | FUNCTION: Hydrolyzes trehalose-6-phosphate to glucose and glucose 6-phosphate. Can also very effectively hydrolyzes p-nitrophenyl-alpha-D-glucopyranoside, but not lactose, maltose, sucrose or sucrose-6-phosphate. Trehalose is also hydrolyzed, but to a much smaller extent than trehalose-6-phosphate. {ECO:0000269|PubMed:7651129, ECO:0000269|PubMed:7751281}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:7751281}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:7751281}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Sequence conflict (8); Site (1) |
| Keywords | Cytoplasm;Glycosidase;Hydrolase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Induced by trehalose and repressed by glucose, fructose or mannitol. {ECO:0000269|PubMed:7651129}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7651129}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 65,184 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23008 |
| Cross Reference Brenda |