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UniProtKB/Swiss-Prot P40926: Variant p.Gly37Arg

Malate dehydrogenase, mitochondrial
Gene: MDH2
Variant information

Variant position:  37
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glycine (G) to Arginine (R) at position 37 (G37R, p.Gly37Arg).
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 glycine (G) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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 DEE51; severe defects in aerobic respiration, when assayed in a heterologous system.
Any additional useful information about the variant.

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



Sequence information

Variant position:  37
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  338
The length of the canonical sequence.

Location on the sequence:   FSTSAQNNAKVAVLGASGGI  G QPLSLLLKNSPLVSRLTLYD
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                         FSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYD

Mouse                         FSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYD

Rat                           FSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYD

Pig                           FSTSXQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYD

Bovine                        FSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYD

Cat                           FSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYD

Caenorhabditis elegans        SVRHSSQAPKVALLGAAGGIGQPLGLLLKQDPLVAHLALYD

Baker's yeast                 FSSTVANPYKVTVLGAGGGIGQPLSLLLKLNHKVTDLRLYD

Fission yeast                 FSTTSSRAFKVAVLGAGGGIGQPLSMLLKLNDKVSELALFD

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 25 – 338 Malate dehydrogenase, mitochondrial
Nucleotide binding 31 – 37 NAD
Binding site 57 – 57 NAD
Glycosylation 33 – 33 O-linked (GlcNAc) serine
Helix 37 – 45


Literature citations

Mutations in MDH2, encoding a Krebs cycle enzyme, cause early-onset severe encephalopathy.
Ait-El-Mkadem S.; Dayem-Quere M.; Gusic M.; Chaussenot A.; Bannwarth S.; Francois B.; Genin E.C.; Fragaki K.; Volker-Touw C.L.; Vasnier C.; Serre V.; van Gassen K.L.; Lespinasse F.; Richter S.; Eisenhofer G.; Rouzier C.; Mochel F.; De Saint-Martin A.; Abi Warde M.T.; de Sain-van der Velde M.G.; Jans J.J.; Amiel J.; Avsec Z.; Mertes C.; Haack T.B.; Strom T.; Meitinger T.; Bonnen P.E.; Taylor R.W.; Gagneur J.; van Hasselt P.M.; Roetig A.; Delahodde A.; Prokisch H.; Fuchs S.A.; Paquis-Flucklinger V.;
Am. J. Hum. Genet. 100:151-159(2017)
Cited for: INVOLVEMENT IN DEE51; VARIANTS DEE51 ARG-37; LEU-133 AND LEU-207; CHARACTERIZATION OF VARIANTS DEE51 LEU-133 AND LEU-207; CATALYTIC ACTIVITY;

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.