Variant position: 479 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 509 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 GAGEMVNEAALALEYGASCE DIARVCHAHPTLSEAFREANL
Mouse GAGEMVNEAALALEYGASCE DIARVCHAHPTLSEAFREANL
Rat GAGEMVNEAALALEYGASCE DVARVCHAHPTLSEAFREANL
Pig GAGEMINEAALALEYGASCE DIARVCHAHPTLSEAFREANL
Caenorhabditis elegans NAGEMIAEATLAMEYGASAE DVARVCHPHPTLSEAFREANL
Slime mold NAGELIGECVLAMEYGASCE DIARTCHGHPTLSEAVKEAAM
Baker's yeast NAGEMIAEAGLALEYGASAE DVARVCHAHPTLSEAFKEANM
Fission yeast MAGELIGEATLALEYGASAE DVARVCHAHPTLSEATKEAMM
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
36 – 509 Dihydrolipoyl dehydrogenase, mitochondrial
487 – 487 Proton acceptor
473 – 473 Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex
466 – 466 E -> A. Decreases dehydrogenase activity. Loss of proteolytic activity.
473 – 473 Y -> A. Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
473 – 473 Y -> F. Does not affect dihydrolipoyl dehydrogenase activity.
473 – 473 Y -> H. Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
482 – 482 R -> A. Does not affect dihydrolipoyl dehydrogenase activity.
482 – 482 R -> M. Does not affect interaction with PDHX.
485 – 485 H -> A. Loss of dehydrogenase activity. Increases proteolytic activity.
491 – 491 S -> A. Loss of proteolytic activity. Does not affect dehydrogenase activity.
492 – 492 E -> Q. Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
477 – 482
Lipoamide dehydrogenase deficiency due to a novel mutation in the interface domain.
Shany E.; Saada A.; Landau D.; Shaag A.; Hershkovitz E.; Elpeleg O.N.;
Biochem. Biophys. Res. Commun. 262:163-166(1999)
Cited for: VARIANT DLDD VAL-479;
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