Sequence information
Variant position: 145 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 403 The length of the canonical sequence.
Location on the sequence:
GILDDLIVTNTSEGHLYVVS
N AGCWEKDLALMQDKVRELQN
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 GILDDLIVTNT-SEGHLYVVSN AGCWEKDLALMQDKVRELQ--N
GIEDDLIVTST-SEGYLYVVSN AGCWDKDLALMQGKVRELQ
Mouse GILDDLIVSNT-SEGHLYVVSN AGCRDKDLALMQDKVKEFQ
Bovine GILDDLIVTSA-SEGHLYVVSN AGCREKDLTLMQDKVRELQ
Chicken DIVDDLIVTNT-AEDHLYVVSN AGCADKDRAVMEGRAAELR
Slime mold GIIDDTMITN--AGDSLYVVVN AGCADKDISHINEKIKEFK
Baker's yeast GVVDDTIITKENDDNEFYIVTN AGCAERDTEFFHDELQNGS
Fission yeast GIIDDTIISKQ-DENTYYIVTN AACSEKDEANLKKHIENWK
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
29 – 403
Aminomethyltransferase, mitochondrial
Alternative sequence
113 – 156
Missing. In isoform 3.
Mutagenesis
129 – 129
D -> AN. Loss of aminomethyltransferase activity.
Literature citations
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.
Okamura-Ikeda K.; Hosaka H.; Yoshimura M.; Yamashita E.; Toma S.; Nakagawa A.; Fujiwara K.; Motokawa Y.; Taniguchi H.;
J. Mol. Biol. 351:1146-1159(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-403 ALONE AND IN COMPLEX WITH 5-METHYLTETRAHYDROFOLATE; SUBSTRATE-BINDING SITES; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS NKH ILE-145; ASP-269 AND HIS-320; MUTAGENESIS OF ASP-129;
Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH).
Toone J.R.; Applegarth D.A.; Coulter-Mackie M.B.; James E.R.;
Mol. Genet. Metab. 72:322-325(2001)
Cited for: VARIANTS NKH ILE-145 AND HIS-320;
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.