Variant position: 233 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 325 The length of the canonical sequence.
Location on the sequence:
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 IMKDMLSAVMQEVPLAALAV HCHDTYGQALANTLMALQMGV
Mouse LMKDMLTAVMHEVPVTALAV HCHDTYGQALANTLVALQMGV
Rat LMKDMLTAVLHEVPVAALAV HCHDTYGQALANTLVALQMGV
Bovine AMKDMLSAVLQEVPVTALAV HCHDTYGQALANTLTALQMGV
Chicken SMKEMLAAVMKEVPVGALAV HCHDTYGQALANILVALQMGV
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.
Type Positions Description
28 – 325 Hydroxymethylglutaryl-CoA lyase, mitochondrial
33 – 300 Pyruvate carboxyltransferase
233 – 233
235 – 235
188 – 250 Missing. In isoform 3.
233 – 233 H -> A. Loss of activity, and reduced proton exchange rate.
230 – 235
Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine-233 as an active site residue.
Roberts J.; Mitchell G.A.; Miziorko H.M.;
J. Biol. Chem. 271:24604-24609(1996)
Cited for: VARIANT HMGCLD ARG-233;
Two missense point mutations in different alleles in the 3-hydroxy-3-methylglutaryl coenzyme A lyase gene produce 3-hydroxy-3-methylglutaric aciduria in a French patient.
Zapater N.; Pie J.; Lloberas J.; Rolland M.O.; Leroux B.; Vidailhet M.; Divry P.; Hegardt F.G.; Casals N.;
Arch. Biochem. Biophys. 358:197-203(1998)
Cited for: VARIANTS HMGCLD ARG-233 AND PRO-263;
Ten novel HMGCL mutations in 24 patients of different origin with 3-hydroxy-3-methyl-glutaric aciduria.
Menao S.; Lopez-Vinas E.; Mir C.; Puisac B.; Gratacos E.; Arnedo M.; Carrasco P.; Moreno S.; Ramos M.; Gil M.C.; Pie A.; Ribes A.; Perez-Cerda C.; Ugarte M.; Clayton P.T.; Korman S.H.; Serra D.; Asins G.; Ramos F.J.; Gomez-Puertas P.; Hegardt F.G.; Casals N.; Pie J.;
Hum. Mutat. 30:E520-E529(2009)
Cited for: VARIANTS HMGCLD LYS-37; GLY-42; PHE-142; TYR-174; SER-192; PHE-200 AND ARG-233; CHARACTERIZATION OF VARIANTS HMGCLD LYS-37; PHE-142; TYR-174; SER-192 AND PHE-200;
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.