Sequence information
Variant position: 193 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 421 The length of the canonical sequence.
Location on the sequence:
KTKAEKKGDEYIINGQKMWI
T NGGKANWYFLLARSDPDPKA
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KTKAEKKGDEYIINGQKMWIT NGGKANWYFLLARSDPDPKA
Chimpanzee KTKAEKKGDEYIINGQKMWIT NGGKANWYFLLARSDPDPKA
Mouse KTKAEKKGDEYVINGQKMWIT NGGKANWYFLLARSNPDPKV
Rat KTKAEKKGDEYVINGQKMWIT NGGKANWYFVLTRSNPDPKV
Pig KTKAEKKGDEYIINGQKMWIT NGGKANWYFLLARSDPDPKA
Bovine KTKAEKKGDEYIINGQKMWIT NGGKANWYFLLARSDPDPKA
Caenorhabditis elegans KTKCEKKGDEYIINGSKAWIT GGGHAKWFFVLARSDPNPKT
Drosophila KTRAEKKGDEWVINGQKMWIT NGGVANWYFVLARTNPDPKC
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
26 – 421
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Nucleotide binding
191 – 193
FAD
Modified residue
179 – 179
N6-succinyllysine
Modified residue
212 – 212
N6-acetyllysine; alternate
Modified residue
212 – 212
N6-succinyllysine; alternate
Mutagenesis
191 – 191
W -> A. Loss of electron transfer to ETF.
Mutagenesis
191 – 191
W -> F. Reduces rate of electron transfer to ETF about six-fold.
Beta strand
182 – 193
Literature citations
The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype?
Andresen B.S.; Bross P.; Udvari S.; Kirk J.; Gray G.; Kmoch S.; Chamoles N.; Knudsen I.; Winter V.; Wilcken B.; Yokota I.; Hart K.; Packman S.; Harpey J.P.; Saudubray J.-M.; Hale D.E.; Bolund L.; Koelvraa S.; Gregersen N.;
Hum. Mol. Genet. 6:695-707(1997)
Cited for: VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352;
Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site.
Kuchler B.; Abdel-Ghany A.G.; Bross P.; Nandy A.; Rasched I.; Ghisla S.;
Biochem. J. 337:225-230(1999)
Cited for: CHARACTERIZATION OF VARIANT ACADMD ALA-193;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.