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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P11310: Variant p.Lys329Glu

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene: ACADM
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Variant information Variant position: help 329 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 Lysine (K) to Glutamate (E) at position 329 (K329E, p.Lys329Glu). 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 large size and basic (K) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 ACADMD; may alter splicing; decreased fatty acid beta-oxidation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 329 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 421 The length of the canonical sequence.
Location on the sequence: help FGKLLVEHQAISFMLAEMAM K VELARMSYQRAAWEVDSGRR 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                         FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR

Chimpanzee                    FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR

Mouse                         FGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRR

Rat                           FGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRR

Pig                           FGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRR

Bovine                        FGKLLIEHQGISFLLAEMAMKVELARLSYQRAAWEVDSGRR

Caenorhabditis elegans        FGTVIANHQAVQFMLADMAVNLELARLITYKSANDVDNKVR

Drosophila                    FGVPIAYHQAVQFMLADMAIGVETSRLAWRLSAWEIDQGRR
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 26 – 421 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Helix 317 – 345



Literature citations
Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency.
Matsubara Y.; Narisawa K.; Miyabayashi S.; Tada K.; Coates P.M.; Bachmann C.; Elsas L.J. II; Pollitt R.J.; Rhead W.J.; Roe C.R.;
Biochem. Biophys. Res. Commun. 171:498-505(1990)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342; VARIANT ACADMD GLU-329; Medium chain acyl-CoA dehydrogenase, K304E mutant.
Battaile K.P.; Mohsen A.-W.; Vockley J.;
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 35-421 OF VARIANT ACADMD GLU-329 IN COMPLEX WITH FAD; COFACTOR; SUBUNIT; Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation.
Yokota I.; Indo Y.; Coates P.M.; Tanaka K.;
J. Clin. Invest. 86:1000-1003(1990)
Cited for: VARIANT ACADMD GLU-329; Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency.
Kelly D.P.; Whelan A.J.; Ogden M.L.; Alpers R.; Zhang Z.F.; Bellus G.; Gregersen N.; Dorland L.; Strauss A.W.;
Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990)
Cited for: VARIANT ACADMD GLU-329; FUNCTION; PATHWAY; Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli.
Gregersen N.; Andresen B.S.; Bross P.; Winter V.; Ruediger N.; Engst S.; Christensen E.; Kelly D.; Strauss A.W.; Koelvraa S.; Bolund L.; Ghisla S.;
Hum. Genet. 86:545-551(1991)
Cited for: VARIANT ACADMD GLU-329; Frequency of the G985 MCAD mutation in the general population.
Blakemore A.I.; Singleton H.; Pollitt R.J.; Engel P.C.; Kolvraa S.; Gregersen N.; Curtis D.;
Lancet 337:298-299(1991)
Cited for: VARIANT ACADMD GLU-329; Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency.
Yang B.-Z.; Ding J.-H.; Zhou C.; Dimachkie M.M.; Sweetman L.; Dasouki M.J.; Wilkinson J.; Roe C.R.;
Mol. Genet. Metab. 69:259-262(2000)
Cited for: VARIANTS ACADMD LEU-206 AND GLU-329; Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency.
Albers S.; Levy H.L.; Irons M.; Strauss A.W.; Marsden D.;
J. Inherit. Metab. Dis. 24:417-418(2001)
Cited for: VARIANTS ACADMD THR-281 AND GLU-329;
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.