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:
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 GGMGFMKEPGVERVLRDLRI FRIFEGTNDILRLFVALQGCM
Mouse GGMGFMKEPGVERVLRDIRI FRIFEGANDILRLFVALQGCM
Rat GGMGFMKEPGVERVLRDIRI FRIFEGTNDILRLFVALQGCM
Bovine GGMGFMKEPGVERVLRDLRI FRIFEGTNDILRLFVALQGCM
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
41 – 655 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
41 – 482 Catalytic
462 – 462 Proton acceptor
458 – 458 F -> T. Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.
458 – 458 F -> V. Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.
458 – 458 F -> Y. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
462 – 462 E -> D. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.
462 – 462 E -> Q. Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
456 – 459
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.;
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;
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