| IED ID | IndEnz0002006649 |
| Enzyme Type ID | protease006649 |
| Protein Name |
tRNA N6-adenosine threonylcarbamoyltransferase EC 2.3.1.234 N6-L-threonylcarbamoyladenine synthase t 6 A synthase Pombe glycoprotease 2 t 6 A37 threonylcarbamoyladenosine biosynthesis protein kae1 tRNA threonylcarbamoyladenosine biosynthesis protein kae1 |
| Gene Name | pgp2 kae1 SPBC16D10.03 |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MGKPLIALGLEGSANKLGVGIILHDTNGSAKILANVRHTYITPPGQGFLPSDTAKHHRAWIIPLIKQAFAEAKISFKDIDCICFTKGPGIGAPLNSVALCARMLSLIHKKPLVAVNHCIGHIEMGREITGAQNPVVLYVSGGNTQVIAYSEKKYRIFGETLDIAIGNCLDRFARIIGLSNAPSPGYNIMQEAKKGKRFIELPYTVKGMDCSFSGLLSGVEAAATELLDPKNPSSVTKQDLCYSLQETGFAMLVEITERAMAHIRADSVLIVGGVGCNERLQQMMAEMSSDRGADVFSTDERFCIDNGIMIAQAGLLAYKTGDRCAVAESTITQRYRTDDVYISWRD |
| Enzyme Length | 346 |
| Uniprot Accession Number | O94637 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 170; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03180; BINDING 185; /note=Substrate; via amide nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03180; BINDING 277; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03180 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; Evidence={ECO:0000255|HAMAP-Rule:MF_03180}; |
| DNA Binding | |
| EC Number | 2.3.1.234 |
| Enzyme Function | FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Pgp2 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. {ECO:0000255|HAMAP-Rule:MF_03180}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Metal binding (4); Region (1) |
| Keywords | Activator;Acyltransferase;Cytoplasm;Metal-binding;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase;tRNA processing |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:16823372}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 23697806; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,515 |
| Kinetics | |
| Metal Binding | METAL 117; /note=Divalent metal cation; /evidence=ECO:0000255|HAMAP-Rule:MF_03180; METAL 121; /note=Divalent metal cation; /evidence=ECO:0000255|HAMAP-Rule:MF_03180; METAL 138; /note=Divalent metal cation; /evidence=ECO:0000255|HAMAP-Rule:MF_03180; METAL 305; /note=Divalent metal cation; /evidence=ECO:0000255|HAMAP-Rule:MF_03180 |
| Rhea ID | RHEA:37059 |
| Cross Reference Brenda |