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UniProtKB/Swiss-Prot P11310: Variant p.Thr193Ala

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene: ACADM
Variant information

Variant position:  193
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Threonine (T) to Alanine (A) at position 193 (T193A, p.Thr193Ala).
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:  Change from medium size and polar (T) to small size and hydrophobic (A)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In ACADMD; the thermostability is markedly decreased.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  193
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  421
The length of the canonical sequence.

Location on the sequence:   KTKAEKKGDEYIINGQKMWI  T NGGKANWYFLLARSDPDPKA
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                         KTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKA

Chimpanzee                    KTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKA

Mouse                         KTKAEKKGDEYVINGQKMWITNGGKANWYFLLARSNPDPKV

Rat                           KTKAEKKGDEYVINGQKMWITNGGKANWYFVLTRSNPDPKV

Pig                           KTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKA

Bovine                        KTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKA

Caenorhabditis elegans        KTKCEKKGDEYIINGSKAWITGGGHAKWFFVLARSDPNPKT

Drosophila                    KTRAEKKGDEWVINGQKMWITNGGVANWYFVLARTNPDPKC

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.

TypePositionsDescription
Chain 26 – 421 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Nucleotide binding 191 – 193 FAD
Modified residue 179 – 179 N6-succinyllysine
Modified residue 212 – 212 N6-acetyllysine; alternate
Modified residue 212 – 212 N6-succinyllysine; alternate
Mutagenesis 191 – 191 W -> A. Loss of electron transfer to ETF.
Mutagenesis 191 – 191 W -> F. Reduces rate of electron transfer to ETF about six-fold.
Beta strand 182 – 193


Literature citations

The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype?
Andresen B.S.; Bross P.; Udvari S.; Kirk J.; Gray G.; Kmoch S.; Chamoles N.; Knudsen I.; Winter V.; Wilcken B.; Yokota I.; Hart K.; Packman S.; Harpey J.P.; Saudubray J.-M.; Hale D.E.; Bolund L.; Koelvraa S.; Gregersen N.;
Hum. Mol. Genet. 6:695-707(1997)
Cited for: VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352;

Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site.
Kuchler B.; Abdel-Ghany A.G.; Bross P.; Nandy A.; Rasched I.; Ghisla S.;
Biochem. J. 337:225-230(1999)
Cited for: CHARACTERIZATION OF VARIANT ACADMD ALA-193;

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.