UniProtKB/Swiss-Prot Q96HY7: Variant p.Pro773Leu

2-oxoadipate dehydrogenase complex component E1
Gene: DHTKD1
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Variant information Variant position:

773 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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:

From Proline (P) to Leucine (L) at position 773 (P773L, p.Pro773Leu). 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:

Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-3 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 AAKAD; uncertain significance; thermally more labile than wild-type protein. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs200355418 [ dbSNP | Ensembl ]

Sequence information Variant position:

773 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

919 The length of the canonical sequence.
Location on the sequence:

MVRNFRKPLIVASPKMLLRL P AAVSTLQEMAPGTTFNPVIG 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                         MVRNFRKPLIVASPKMLLRLPAAVSTLQEMAPGTTFNPVIG

Mouse                         MIRNFRKPLIVASPKMLLRYPAAVSTLEEMAPGTAFKPVIG

Rat                           MMRNFRKPLIVASPKMLLRYPVAVSTLEEMAPGTAFKPVIG

Xenopus laevis                MVRSFRKPLIVASPKMLLRYPAAVSSLEDIAPGKTFRSVIG

Zebrafish                     MIRNFRKPLIVASPKTLLRFSGAVSGLSDMGPGTSFKPIIG

Caenorhabditis elegans        VVPNYRKPLIVVGPKILLRHPKAASTINEFGPGTTYQNVIS

Drosophila                    LARNFRKPLVVVAPKTLLRLPAATSTHEDFQPGTLFHNVLG

Slime mold                    MIRNYRKPLIVAGPKVLLRHPNCFSTLNEMAPGTHFQTVLS

Literature citations
Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism.
Bezerra G.A.; Foster W.R.; Bailey H.J.; Hicks K.G.; Sauer S.W.; Dimitrov B.; McCorvie T.J.; Okun J.G.; Rutter J.; Koelker S.; Yue W.W.;
IUCrJ 7:693-706(2020)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; PATHWAY; COFACTOR; X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 45-919; INTERACTION WITH DLST; CHARACTERIZATION OF VARIANTS AAKAD CYS-715 AND LEU-773; Genetic basis of alpha-aminoadipic and alpha-ketoadipic aciduria.
Hagen J.; te Brinke H.; Wanders R.J.; Knegt A.C.; Oussoren E.; Hoogeboom A.J.; Ruijter G.J.; Becker D.; Schwab K.O.; Franke I.; Duran M.; Waterham H.R.; Sass J.O.; Houten S.M.;
J. Inherit. Metab. Dis. 38:873-879(2015)
Cited for: VARIANTS AAKAD GLY-234; 437-GLU--ALA-919 DEL; GLN-455; LEU-773 AND PRO-777;

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.