Sequence information
Variant position: 301 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 427 The length of the canonical sequence.
Location on the sequence:
ANASTLNDGAAALVLMTADA
A KRLNVTPLARIVAFADAAVE
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 ANASTLNDGAAALVLMTADAA KRLNVTPLARIVAFADAAVE
Mouse ANASTLNDGAAALVLMTAEAA QRLNVKPLARIAAFADAAVD
Rat ANASTLNDGAAAVVLMTAEAA QRLKVKPLARIAAFADAAVD
Bovine ANASTLNDGAAAVVLMTADAA KRLNVKPLARIAAFADAAVE
Xenopus tropicalis ANASTLNDGAAALVLMTAGAA SRLNVTPLARIVAFADAAVD
Zebrafish ANASTLNDGAAALVLMTADAA QRLNVTPLAKIVAFADAAVA
Baker's yeast ANASPINDGAAAVILVSEKVL KEKNLKPLAIIKGWGEAAHQ
Fission yeast ANASTLNDGASALVLMSAAKV KELGLKPLAKIIGWGEAAQD
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
Chain
34 – 427
Acetyl-CoA acetyltransferase, mitochondrial
Metal binding
281 – 281
Potassium; via carbonyl oxygen
Metal binding
283 – 283
Potassium; via carbonyl oxygen
Binding site
284 – 284
Coenzyme A
Alternative sequence
163 – 427
Missing. In isoform 2.
Helix
298 – 303
Literature citations
Molecular, biochemical, and clinical characterization of mitochondrial acetoacetyl-coenzyme A thiolase deficiency in two further patients.
Wakazono A.; Fukao T.; Yamaguchi S.; Hori T.; Orii T.; Lambert M.; Mitchell G.A.; Lee G.W.; Hashimoto T.;
Hum. Mutat. 5:34-42(1995)
Cited for: VARIANTS 3KTD ASP-158; MET-297 AND PRO-301; CHARACTERIZATION OF VARIANTS 3KTD ASP-158; MET-297 AND PRO-301; FUNCTION; CATALYTIC ACTIVITY; 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.