| IED ID | IndEnz0002013832 |
| Enzyme Type ID | protease013832 |
| Protein Name |
tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial EC 2.3.1.234 N6-L-threonylcarbamoyladenine synthase t 6 A synthase Pombe glycoprotease 1 t 6 A37 threonylcarbamoyladenosine biosynthesis protein pgp1 tRNA threonylcarbamoyladenosine biosynthesis protein pgp1 |
| Gene Name | pgp1 SPCC1259.10 |
| 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 | MLCLVYNSILCKQRRISLKVLQQFRCWNISKTFLSYRTLTALAIETSCDDTSVSVVRTSDSSSHCQNEIICLNTHRTISKYEAYGGIHPTIVIHEHQKNLAKVIQRTISDAARSGITDFDLIAVTRGPGMIGPLAVGLNTAKGLAVGLQKPLLAVHHMQAHALAVQLEKSIDFPYLNILVSGGHTMLVYSNSLLNHEIIVTTSDIAVGDYLDKCAKYLGIPWDNEMPAAALEQFASPEINSTSYSLKPPIPLNTREKVHSASFSFSGLESYACRIIRKTPLNLSEKKFFAYQLQYAAFQHICQKTLLALKRLDLSKVKYLVCSGGVARNELLKKMLNDTLMVLQFEHQPTDIKLVYPSPDICSDNAAMIGYTAIQMFKAGYTSSFDVEPIRKWPINQILTVEGWLTKKNKKV |
| Enzyme Length | 412 |
| Uniprot Accession Number | O94710 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 212; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03179; BINDING 228; /note=Substrate; via amide nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03179; BINDING 232; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03179; BINDING 363; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03179 |
| 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_03179}; |
| DNA Binding | |
| EC Number | 2.3.1.234 |
| Enzyme Function | FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. {ECO:0000255|HAMAP-Rule:MF_03179}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (4); Chain (1); Metal binding (3); Region (2); Transit peptide (1) |
| Keywords | Acyltransferase;Metal-binding;Mitochondrion;Reference proteome;Transferase;Transit peptide;tRNA processing |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:16823372}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16491466; 16802154; 18684775; 20473289; 23697806; 25803873; 28410370; 29996109; 34250083; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,973 |
| Kinetics | |
| Metal Binding | METAL 157; /note=Divalent metal cation; /evidence=ECO:0000255|HAMAP-Rule:MF_03179; METAL 161; /note=Divalent metal cation; /evidence=ECO:0000255|HAMAP-Rule:MF_03179; METAL 364; /note=Divalent metal cation; /evidence=ECO:0000255|HAMAP-Rule:MF_03179 |
| Rhea ID | RHEA:37059 |
| Cross Reference Brenda |