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UniProtKB/Swiss-Prot P11310: Variant p.Lys329Glu

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

Variant position:  329
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 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:  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:  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

Involvement in disease:  Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:201450]: An inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy. {ECO:0000269|PubMed:10767181, ECO:0000269|PubMed:11349232, ECO:0000269|PubMed:11409868, ECO:0000269|PubMed:11486912, ECO:0000269|PubMed:1363805, ECO:0000269|PubMed:1671131, ECO:0000269|PubMed:1684086, ECO:0000269|PubMed:1902818, ECO:0000269|PubMed:2251268, ECO:0000269|PubMed:2393404, ECO:0000269|PubMed:2394825, ECO:0000269|PubMed:7603790, ECO:0000269|PubMed:7929823, ECO:0000269|PubMed:8198141, ECO:0000269|PubMed:9158144, ECO:0000269|PubMed:9882619}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In ACADMD; most common variant.
Any additional useful information about the variant.

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



Sequence information

Variant position:  329
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:   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: 
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:  
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;

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;

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 FREQUENCY;

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.