Variant position:  329

Type of variant:  LP/P [Disclaimer: Variants classification is intended for research purposes only, not for clinical and diagnostic use. The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant.]

Residue change:  From Lysine (K) to Glutamate (E) at position 329 (K329E, p.Lys329Glu).

Physico-chemical properties:  Change from large size and basic (K) to medium size and acidic (E)

BLOSUM score:  1

Variant description:  In ACADMD; may alter splicing; decreased fatty acid beta-oxidation.

Other resources:  

• Variant rs77931234 [ dbSNP | Ensembl ]

Variant position:  329

Protein sequence length:  421

Location on the sequence:   FGKLLVEHQAISFMLAEMAM  K VELARMSYQRAAWEVDSGRR

Residue conservation: 

Human                         FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR

Chimpanzee                    FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR

Mouse                         FGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRR

Rat                           FGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRR

Pig                           FGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRR

Bovine                        FGKLLIEHQGISFLLAEMAMKVELARLSYQRAAWEVDSGRR

Caenorhabditis elegans        FGTVIANHQAVQFMLADMAVNLELARLITYKSANDVDNKVR

Drosophila                    FGVPIAYHQAVQFMLADMAIGVETSRLAWRLSAWEIDQGRR

Sequence annotation in neighborhood:  

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 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;