Sequence information
Variant position: 458 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 655 The length of the canonical sequence.
Location on the sequence:
GGMGFMKEPGVERVLRDLRI
F RIFEGTNDILRLFVALQGCM
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 GGMGFMKEPGVERVLRDLRIF RIFEGTNDILRLFVALQGCM
Mouse GGMGFMKEPGVERVLRDIRIF RIFEGANDILRLFVALQGCM
Rat GGMGFMKEPGVERVLRDIRIF RIFEGTNDILRLFVALQGCM
Bovine GGMGFMKEPGVERVLRDLRIF RIFEGTNDILRLFVALQGCM
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
41 – 655
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Region
41 – 482
Catalytic
Active site
462 – 462
Proton acceptor
Mutagenesis
458 – 458
F -> T. Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.
Mutagenesis
458 – 458
F -> V. Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.
Mutagenesis
458 – 458
F -> Y. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
Mutagenesis
462 – 462
E -> D. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.
Mutagenesis
462 – 462
E -> Q. Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
Helix
456 – 459
Literature citations
Catalytic and FAD-binding residues of mitochondrial very long chain acyl-coenzyme A dehydrogenase.
Souri M.; Aoyama T.; Cox G.F.; Hashimoto T.;
J. Biol. Chem. 273:4227-4231(1998)
Cited for: FUNCTION; CATALYTIC ACTIVITY; COFACTOR; BIOPHYSICOCHEMICAL PROPERTIES; SUBUNIT; SUBCELLULAR LOCATION; MUTAGENESIS OF PHE-458 AND GLU-462; ACTIVE SITE; CHARACTERIZATION OF VARIANT ACADVLD LEU-458;
Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death.
Mathur A.; Sims H.F.; Gopalakrishnan D.; Gibson B.; Rinaldo P.; Vockley J.; Hug G.; Strauss A.W.;
Circulation 99:1337-1343(1999)
Cited for: VARIANTS ACADVLD GLU-130 DEL; PRO-213; GLU-247; MET-260; LYS-278 DEL; ALA-283; ASP-441; LEU-458; PRO-490; LYS-534; TRP-613 AND GLN-615;
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.