| IED ID | IndEnz0001000382 |
| Enzyme Type ID | amylase000382 |
| Protein Name |
Trehalose-6-phosphate hydrolase EC 3.2.1.93 Alpha,alpha-phosphotrehalase |
| Gene Name | treC olgH b4239 JW4198 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTHLPHWWQNGVIYQIYPKSFQDTTGSGTGDLRGVIQHLDYLHKLGVDAIWLTPFYVSPQVDNGYDVANYTAIDPTYGTLDDFDELVTQAKSRGIRIILDMVFNHTSTQHAWFREALNKESPYRQFYIWRDGEPETPPNNWRSKFGGSAWRWHAESEQYYLHLFAPEQADLNWENPAVRAELKKVCEFWADRGVDGLRLDVVNLISKDPRFPEDLDGDGRRFYTDGPRAHEFLHEMNRDVFTPRGLMTVGEMSSTSLEHCQRYAALTGSELSMTFNFHHLKVDYPGGEKWTLAKPDFVALKTLFRHWQQGMHNVAWNALFWCNHDQPRIVSRFGDEGEYRVPAAKMLAMVLHGMQGTPYIYQGEEIGMTNPHFTRITDYRDVESLNMFAELRNDGRDADELLAILASKSRDNSRTPMQWSNGDNAGFTAGEPWIGLGDNYQQINVEAALADDSSVFYTYQKLIALRKQEAILTWGNYQDLLPNSPVLWCYRREWKGQTLLVIANLSREIQPWQAGQMRGNWQLVMHNYEEASPQPCAMNLRPFEAVWWLQK |
| Enzyme Length | 551 |
| Uniprot Accession Number | P28904 |
| Absorption | |
| Active Site | ACT_SITE 200; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00691; ACT_SITE 251; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P00691 |
| Activity Regulation | |
| 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:8083158}; |
| 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 it does not recognize trehalose, sucrose, maltose, isomaltose, or maltodextrins. {ECO:0000269|PubMed:8083158}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Sequence conflict (1); Site (1) |
| Keywords | Cytoplasm;Glycosidase;Hydrolase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8083158}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16606699; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,838 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6 mM for trehalose-6-phosphate {ECO:0000269|PubMed:8083158}; Vmax=5.5 umol/min/mg enzyme {ECO:0000269|PubMed:8083158}; |
| Metal Binding | |
| Rhea ID | RHEA:23008 |
| Cross Reference Brenda |