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UniProtKB/Swiss-Prot Q14376: Variant p.Val94Met

UDP-glucose 4-epimerase
Gene: GALE
Variant information

Variant position:  94
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 Valine (V) to Methionine (M) at position 94 (V94M, p.Val94Met).
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:  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:  In GALAC3; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine.
Any additional useful information about the variant.

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



Sequence information

Variant position:  94
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  348
The length of the canonical sequence.

Location on the sequence:   QRLFKKYSFMAVIHFAGLKA  V GESVQKPLDYYRVNLTGTIQ
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                         QRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQ

Mouse                         QHLFKKHSFKAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQ

Rat                           QHLFKKHNFKAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQ

Bovine                        QRLFKKHSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQ

Caenorhabditis elegans        EKVFSENKFDGIIHLAALKAVGESVAKPLQYYSNNLVASLN

Drosophila                    RSVFQEHKIDMVAHFAALKAVGESCRIPLQYYHNNMTGTNV

Slime mold                    DEIFETGNIRSVIHFAGLKAVGESNKLPLKYYNNNIAGTLT

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 1 – 348 UDP-glucose 4-epimerase
Binding site 88 – 88 NAD; via carbonyl oxygen
Binding site 92 – 92 NAD
Helix 94 – 99


Literature citations

Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase.
Thoden J.B.; Wohlers T.M.; Fridovich-Keil J.L.; Holden H.M.;
J. Biol. Chem. 276:20617-20623(2001)
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT GALAC3 MET-94 IN COMPLEXES WITH NAD AND THE SUBSTRATE ANALOGS UDP-D-GALACTOSE; UDP-N-ACETYL-ALPHA-D-GLUCOSAMINE; UDP-D-GLUCOSE;

Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia.
Wohlers T.M.; Christacos N.C.; Harreman M.T.; Fridovich-Keil J.L.;
Am. J. Hum. Genet. 64:462-470(1999)
Cited for: VARIANT GALAC3 MET-94; CHARACTERIZATION OF VARIANTS GALAC3 GLU-90; MET-94; GLY-103 AND MET-313;

Studies of the V94M-substituted human UDPgalactose-4-epimerase enzyme associated with generalized epimerase-deficiency galactosaemia.
Wohlers T.M.; Fridovich-Keil J.L.;
J. Inherit. Metab. Dis. 23:713-729(2000)
Cited for: BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANT MET-94;

A PCR-based method for detecting known mutations in the human UDP galactose-4'-epimerase gene associated with epimerase-deficiency galactosemia.
Henderson J.M.; Huguenin S.M.; Cowan T.M.; Fridovich-Keil J.L.;
Clin. Genet. 60:350-355(2001)
Cited for: VARIANTS GALAC3 SER-34; GLU-90; MET-94; GLY-103; PRO-183; ARG-257; MET-313; GLU-319 AND HIS-335;

Functional analysis of disease-causing mutations in human UDP-galactose 4-epimerase.
Timson D.J.;
FEBS J. 272:6170-6177(2005)
Cited for: BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS GALAC3 SER-34; GLU-90; MET-94; GLY-103; PRO-183; ARG-257; MET-313; GLU-319 AND HIS-335; SUBUNIT;

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.