Variant position: 109 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 866 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 TWHAAGLTTYFHPGINLKKI HYDSIKLYEKLEEETGQVVGF
Mouse TWHAAGLTTYFHPGINLKKI HYDSIKLYERLEEETGQVVGF
Rat TWHAAGLTTYFHPGINLKKI HYDSIKLYERLEEETGQVVGF
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
51 – 866 Dimethylglycine dehydrogenase, mitochondrial
91 – 91 Tele-8alpha-FAD histidine
114 – 114 N6-acetyllysine
19 – 398 Missing. In isoform 2.
105 – 123
Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency.
Binzak B.A.; Wevers R.A.; Moolenaar S.H.; Lee Y.-M.; Hwu W.-L.; Poggi-Bach J.; Engelke U.F.H.; Hoard H.M.; Vockley J.G.; Vockley J.;
Am. J. Hum. Genet. 68:839-847(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS GLY-530 AND PRO-646; VARIANT DMGDHD ARG-109;
Structure and biochemical properties of recombinant human dimethylglycine dehydrogenase and comparison to the disease-related H109R variant.
Augustin P.; Hromic A.; Pavkov-Keller T.; Gruber K.; Macheroux P.;
FEBS J. 283:3587-3603(2016)
Cited for: X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) OF 29-866 IN COMPLEX WITH FAD; CHARACTERIZATION OF VARIANT DMGDHD ARG-109; FUNCTION; CATALYTIC ACTIVITY; COFACTOR; BIOPHYSICOCHEMICAL PROPERTIES; ENZYME KINETICS;
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.