MTFMT
Domain
Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.
Function
Methionyl-tRNA formyltransferase that formylates methionyl-tRNA in mitochondria and is crucial for translation initiation.
Involvement in disease
Combined oxidative phosphorylation deficiency 15
COXPD15
An autosomal recessive, mitochondrial, neurologic disorder characterized by features of Leigh syndrome and combined oxidative phosphorylation deficiency. Clinical features include mild global developmental delay, white matter abnormalities, ataxia, incoordination, speech and reading difficulties, T2-weighted hyperintensities in the basal ganglia, corpus callosum, and brainstem.
None
The disease is caused by variants affecting the gene represented in this entry.
Mitochondrial complex I deficiency, nuclear type 27
MC1DN27
A form of mitochondrial complex I deficiency, the most common biochemical signature of mitochondrial disorders, a group of highly heterogeneous conditions characterized by defective oxidative phosphorylation, which collectively affects 1 in 5-10000 live births. Clinical disorders have variable severity, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. MC1DN27 transmission pattern is consistent with autosomal recessive inheritance.
None
The disease is caused by variants affecting the gene represented in this entry.
Sequence Similarities
Belongs to the Fmt family.
Cellular localization
- Mitochondrion
Alternative names
FMT, FMT1, MTFMT, MtFMT