| IED ID | IndEnz0004000089 |
| Enzyme Type ID | xylanase000089 |
| Protein Name |
Transketolase TK EC 2.2.1.1 |
| Gene Name | tkt tktA BSU17890 |
| 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 | MDTIEKKSVATIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTKFMNVSPANPGWFNRDRFVLSAGHGSALLYSMLHLSGFDLSIEDLKGFRQWGSKTPGHPEFGHTAGVDATTGPLGQGIAMAVGMAIAERHLAETYNRDSFNVVDHYTYSICGDGDLMEGISSEAASLAGHLQLGRLIVLYDSNDISLDGDLDRSFSENVKQRFEAMNWEVLYVEDGNNIEELTAAIEKARQNEKKPTLIEVKTTIGFGSPNRAGTSGVHGAPLGKEESKLTKEAYAWTYEEDFYVPSEVYEHFAVAVKESGEKKEQEWNAQFAKYKEVYPELAEQLELAIKGELPKDWDQEVPVYEKGSSLASRASSGEVLNGLAKKIPFFVGGSADLAGSNKTTIKNAGDFTAVDYSGKNFWFGVREFAMGAALNGMALHGGLRVFGGTFFVFSDYLRPAIRLAALMGLPVTYVFTHDSIAVGEDGPTHEPVEQLASLRAMPNLSLIRPADGNETAAAWKLAVQSTDHPTALVLTRQNLPTIDQTSEEALAGVEKGAYVVSKSKNETPDALLIASGSEVGLAIEAQAELAKENIDVSVVSMPSMDRFEKQSDEYKNEVLPADVKKRLAIEMGSSFGWGKYTGLEGDVLGIDRFGASAPGETIINEYGFSVPNVVNRVKALINK |
| Enzyme Length | 667 |
| Uniprot Accession Number | P45694 |
| Absorption | |
| Active Site | ACT_SITE 411; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 27; /note=Substrate; /evidence=ECO:0000250; BINDING 67; /note=Thiamine pyrophosphate; /evidence=ECO:0000250; BINDING 157; /note=Thiamine pyrophosphate; via amide nitrogen; /evidence=ECO:0000250; BINDING 186; /note=Thiamine pyrophosphate; /evidence=ECO:0000250; BINDING 262; /note=Substrate; /evidence=ECO:0000250; BINDING 262; /note=Thiamine pyrophosphate; /evidence=ECO:0000250; BINDING 357; /note=Substrate; /evidence=ECO:0000250; BINDING 384; /note=Substrate; /evidence=ECO:0000250; BINDING 437; /note=Thiamine pyrophosphate; /evidence=ECO:0000250; BINDING 461; /note=Substrate; /evidence=ECO:0000250; BINDING 469; /note=Substrate; /evidence=ECO:0000250; BINDING 520; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; |
| DNA Binding | |
| EC Number | 2.2.1.1 |
| Enzyme Function | FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 115..117; /note=Thiamine pyrophosphate; /evidence=ECO:0000250 |
| Features | Active site (1); Binding site (12); Chain (1); Metal binding (3); Nucleotide binding (1); Site (2) |
| Keywords | Calcium;Magnesium;Metal-binding;Reference proteome;Thiamine pyrophosphate;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16796675; 22512862; |
| Motif | |
| Gene Encoded By | |
| Mass | 72,344 |
| Kinetics | |
| Metal Binding | METAL 156; /note=Magnesium; /evidence=ECO:0000250; METAL 186; /note=Magnesium; /evidence=ECO:0000250; METAL 188; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | RHEA:10508 |
| Cross Reference Brenda |