Variant position: 482 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 EMVNEAALALEYGASCEDIA RVCHAHPTLSEAFREANLAAS
Mouse EMVNEAALALEYGASCEDIA RVCHAHPTLSEAFREANLAAA
Rat EMVNEAALALEYGASCEDVA RVCHAHPTLSEAFREANLAAS
Pig EMINEAALALEYGASCEDIA RVCHAHPTLSEAFREANLAAS
Caenorhabditis elegans EMIAEATLAMEYGASAEDVA RVCHPHPTLSEAFREANLAAY
Slime mold ELIGECVLAMEYGASCEDIA RTCHGHPTLSEAVKEAAMDAY
Baker's yeast EMIAEAGLALEYGASAEDVA RVCHAHPTLSEAFKEANMAAY
Fission yeast ELIGEATLALEYGASAEDVA RVCHAHPTLSEATKEAMMAAW
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
502 – 502 Phosphoserine
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
A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency.
Odievre M.H.; Chretien D.; Munnich A.; Robinson B.H.; Dumoulin R.; Masmoudi S.; Kadhom N.; Roetig A.; Rustin P.; Bonnefont J.P.;
Hum. Mutat. 25:323-324(2005)
Cited for: VARIANT DLDD GLY-482; CHARACTERIZATION OF VARIANT DLDD GLY-482; CATALYTIC ACTIVITY;
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.