Search Results
Overview
| Uniprot ID | P21549 |
|---|---|
| Protein Name | Alanine--glyoxylate aminotransferase |
| Gene Name | AGXT |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 12 | KLLVTPPKALLKPLS |
| 128 | ARVHPMTKDPGGHYT |
| 16 | TPPKALLKPLSIPNQ |
| 225 | SLISFSDKAKKKMYS |
| 234 | KKKMYSRKTKPFSFY |
| 312 | LGLQLFVKDPALRLP |
| 389 | AALQHCPKKKL**** |
| 5 | ***MASHKLLVTPPK |
Function
Peroxisomal aminotransferase that catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification (PubMed:10960483, PubMed:12777626, PubMed:23229545, PubMed:24055001, PubMed:26149463). Also catalyzes the transamination between L-serine and pyruvate and contributes to gluconeogenesis from the L-serine metabolism (PubMed:10347152)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005782 | peroxisomal matrix |
| Cellular Component | GO:0005777 | peroxisome |
| Molecular Function | GO:0008453 | alanine-glyoxylate transaminase activity |
| Molecular Function | GO:0016597 | amino acid binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0004760 | L-serine-pyruvate transaminase activity |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0030170 | pyridoxal phosphate binding |
| Molecular Function | GO:0008483 | transaminase activity |
| Biological Process | GO:0019265 | glycine biosynthetic process, by transamination of glyoxylate |
| Biological Process | GO:0009436 | glyoxylate catabolic process |
| Biological Process | GO:0046487 | glyoxylate metabolic process |
| Biological Process | GO:0042853 | L-alanine catabolic process |
| Biological Process | GO:0019448 | L-cysteine catabolic process |
| Biological Process | GO:0006563 | L-serine metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.