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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P12694: Variant p.Ala253Thr

2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Gene: BCKDHA
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Variant information Variant position: help 253 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Alanine (A) to Threonine (T) at position 253 (A253T, p.Ala253Thr). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 253 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 445 The length of the canonical sequence.
Location on the sequence: help ICYFGEGAASEGDAHAGFNF A ATLECPIIFFCRNNGYAIST 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         ICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAIST

Chimpanzee                    ICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAIST

Mouse                         ICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAIST

Bovine                        ICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAIST

Caenorhabditis elegans        VVYFGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAIST

Slime mold                    IVYFGEGAASEGDFHAAMNFAAALSTPTIFFCRNNKWAIST
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 46 – 445 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Binding site 238 – 238
Binding site 239 – 239
Binding site 240 – 240
Binding site 265 – 265
Binding site 267 – 267
Binding site 269 – 269
Helix 244 – 255



Literature citations
Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.
Aevarsson A.; Chuang J.L.; Wynn R.M.; Turley S.; Chuang D.T.; Hol W.G.J.;
Structure 8:277-291(2000)
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-445 IN COMPLEX WITH BCKDHB; THIAMINE PYROPHOSPHATE; POTASSIUM AND MAGNESIUM; FUNCTION; CATALYTIC ACTIVITY; COFACTOR; SUBUNIT; SUBCELLULAR LOCATION; VARIANTS MSUD1A ASP-254 AND HIS-297; CHARACTERIZATION OF VARIANTS MSUD1A SER-159; LYS-190; MET-211; SER-249; THR-253; ASP-254; TRP-265; SER-267; PRO-285; ARG-290; HIS-297; ARG-310; CYS-409; CYS-413 AND ASN-438; Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex.
Nobukuni Y.; Mitsubuchi H.; Hayashida Y.; Ohta K.; Indo Y.; Ichiba Y.; Endo F.; Matsuda I.;
Biochim. Biophys. Acta 1225:64-70(1993)
Cited for: VARIANTS MSUD1A TRP-159; LYS-190; THR-253 AND THR-326;
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.