Variant position: 495 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 ASCEDIARVCHAHPTLSEAF REANLAASFGKSINF-
Mouse ASCEDIARVCHAHPTLSEAF REANLAAAFGKPINF
Rat ASCEDVARVCHAHPTLSEAF REANLAASFGKPINF
Pig ASCEDIARVCHAHPTLSEAF REANLAASFGKAINF
Caenorhabditis elegans ASAEDVARVCHPHPTLSEAF REANLAAYCGKAINN
Slime mold ASCEDIARTCHGHPTLSEAV KEAAMDAY-DKPIHM
Baker's yeast ASAEDVARVCHAHPTLSEAF KEANMAAY-DKAIHC
Fission yeast ASAEDVARVCHAHPTLSEAT KEAMMAAWCGKSIHF
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
502 – 502 Phosphoserine
505 – 505 N6-acetyllysine; alternate
505 – 505 N6-succinyllysine; alternate
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.
505 – 505 K -> M. Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
491 – 503
Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex.
Patel M.S.; Korotchkina L.G.; Sidhu S.;
J. Mol. Catal., B Enzym. 61:2-6(2009)
Cited for: CATALYTIC ACTIVITY; INTERACTION WITH PDHX; MUTAGENESIS OF LYS-89; ARG-482; GLU-492 AND LYS-505; CHARACTERIZATION OF VARIANTS DLDD GLU-72; LYS-375; LEU-488 AND GLY-495;
Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex.
Brautigam C.A.; Wynn R.M.; Chuang J.L.; Machius M.; Tomchick D.R.; Chuang D.T.;
Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 36-509 IN COMPLEX WITH PDHX; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT DLDD GLY-495;
Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency.
Hong Y.S.; Kerr D.S.; Craigen W.J.; Tan J.; Pan Y.; Lusk M.; Patel M.S.;
Hum. Mol. Genet. 5:1925-1930(1996)
Cited for: VARIANT DLDD GLY-495;
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