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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O00764: Variant p.Arg220Gln

Pyridoxal kinase
Gene: PDXK
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Variant information Variant position: help 220 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Glutamine (Q) at position 220 (R220Q, p.Arg220Gln). 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: help Change from large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In HMSN6C; decreased pyridoxal kinase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 220 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 312 The length of the canonical sequence.
Location on the sequence: help IVLGSQRRRNPAGSVVMERI R MDIRKVDAVFVGTGDLFAAM 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         IVLGSQRRRNPAGSVVMERIRMDI-RKVDAVFVGTGDLFAAM

Mouse                         IALGSQRMRKPDGSTVTQRIRMEM-RKVEAVFVGTGDLFAA

Rat                           MALGSQRMRKPDGSTVTQRIRMEM-RKVDPVFVGTGDLFAA

Pig                           IALGSQRTRSPDGSVATQRIRMEI-CKVDAVFVGTGDLFAA

Bovine                        MALGSQRTRAPDGSMVTQRIRMEM-HKVDAVFVGTGDLFAA

Sheep                         MALGSQRTRAPDGSVVTQRIRMEM-HKVDAVFVGTGDLFAA

Caenorhabditis elegans        RCYASVK-----GSHVY---RFTF-PRLVGQFVGTGDTFTS

Slime mold                    IVIGST-INDDDNNNKYNQFKIKVGPKFNDYYTGTGDLLSS

Sequence annotation in neighborhood: help 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 – 312 Pyridoxal kinase
Active site 235 – 235 Proton acceptor
Binding site 233 – 233
Modified residue 213 – 213 Phosphoserine
Mutagenesis 235 – 235 D -> A. 15-fold decrease in pyridoxal kinase activity, and a 7-fold decrease in affinity for pyridoxal.
Mutagenesis 235 – 235 D -> N. 2-fold decrease in pyridoxal kinase activity and pyridoxal affinity.
Beta strand 215 – 224



Literature citations
PDXK mutations cause polyneuropathy responsive to pyridoxal 5'-phosphate supplementation.
Chelban V.; Wilson M.P.; Warman Chardon J.; Vandrovcova J.; Zanetti M.N.; Zamba-Papanicolaou E.; Efthymiou S.; Pope S.; Conte M.R.; Abis G.; Liu Y.T.; Tribollet E.; Haridy N.A.; Botia J.A.; Ryten M.; Nicolaou P.; Minaidou A.; Christodoulou K.; Kernohan K.D.; Eaton A.; Osmond M.; Ito Y.; Bourque P.; Jepson J.E.C.; Bello O.; Bremner F.; Cordivari C.; Reilly M.M.; Foiani M.; Heslegrave A.; Zetterberg H.; Heales S.J.R.; Wood N.W.; Rothman J.E.; Boycott K.M.; Mills P.B.; Clayton P.T.; Houlden H.;
Ann. Neurol. 86:225-240(2019)
Cited for: VARIANTS HMSN6C GLN-220 AND THR-228; CHARACTERIZATION OF VARIANTS HMSN6C GLN-220 AND THR-228; BIOPHYSICOCHEMICAL PROPERTIES; CATALYTIC ACTIVITY; FUNCTION; TISSUE SPECIFICITY; PATHWAY;
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.