Protein Variants | Comment | Organism |
---|---|---|
additional information | enzyme mutations at residues Gly97, Ser174, Arg186, Arg190, Arg191, Glu193, and Gln234 can result in the metabolic disorder known as methylmalonic aciduria, MMA, overview | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | Arg19 in the mitochondrial targeting sequence is important | Homo sapiens | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q96EY8 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA | Homo sapiens | ? | - |
? | |
additional information | only two of the three active sites within the trimer contain the bound ATP substrate, twenty residues at the enzymes N-terminus become ordered upon binding of ATP to form an ATP-binding site and an extended cleft that likely binds cobalamin, cobalamin binding site structure involving residue R186, overview | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | the enzyme forms a tightly associated trimer, where the monomer comprises a five-helix bundle and the active sites lie on the subunit interfaces, invariant residues and their function within the ATR structure, detailed overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
ATP:cobalamin adenosyltransferase | - |
Homo sapiens |
ATR | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | twenty residues at the enzymes N-terminus become ordered upon binding of ATP to form an ATP-binding site, structure, overview | Homo sapiens |