Sequence information
Variant position: 402 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 438 The length of the canonical sequence.
Location on the sequence:
ARQARDMLGGNGISDEYHVI
R HAMNLEAVNTYEGTHDIHAL
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 ARQARDMLGGNGISDEYHVIR HAMNLEAVNTYEGTHDIHAL
Mouse ARQARDILGGNGISDEYHVIR HAMNLEAVNTYEGTHDIHAL
Bovine ARQARDMLGGNGISDEYHVIR HVMNLESVNTYEGTHDIHAL
Caenorhabditis elegans ARKARDMLGGNGIVDEYHIMR HMVNLETVNTYEGTHDVHAL
Slime mold ARQSRDMLGGNGIADEYHVIR HAANLETVNTYEGTHDIHAL
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
45 – 438
Glutaryl-CoA dehydrogenase, mitochondrial
Active site
414 – 414
Proton acceptor
Binding site
415 – 415
Substrate; via amide nitrogen
Mutagenesis
414 – 414
E -> D. Reduced catalytic activity.
Helix
400 – 410
Literature citations
Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH).
Keyser B.; Muehlhausen C.; Dickmanns A.; Christensen E.; Muschol N.; Ullrich K.; Braulke T.;
Hum. Mol. Genet. 17:3854-3863(2008)
Cited for: CHARACTERIZATION OF VARIANTS GA1 GLY-138; TRP-402 AND LYS-414; SUBUNIT;
Molecular analysis of Cypriot patients with Glutaric aciduria type I: Identification of two novel mutations.
Georgiou T.; Nicolaidou P.; Hadjichristou A.; Ioannou R.; Dionysiou M.; Siama E.; Chappa G.; Anastasiadou V.; Drousiotou A.;
Clin. Biochem. 47:1300-1305(2014)
Cited for: VARIANTS GA1 ASP-64; VAL-268; ARG-375; TRP-402 AND MET-429;
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.