Peroxisomal aminotransferase that catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification (PubMed:10960483, PubMed:12777626, PubMed:24055001, PubMed:23229545, PubMed:26149463). Also catalyzes the transamination between L-serine and pyruvate and contributes to gluconeogenesis from the L-serine metabolism (PubMed:10347152). L-serine + pyruvate = 3-hydroxypyruvate + L-alanine glyoxylate + L-alanine = glycine + pyruvate Alanine--glyoxylate aminotransferase activity is inhibited by 1 mM (aminooxy)acetic acid by 97.5%. Optimum pH is 7.5- 8.5. Homodimer. Liver. Polymorphism at position 11 acts synergistically with different mutations in AGXT producing specific enzymatic phenotypes in HP1 patients. The combined presence of Leu-11 and Met-340 polymorphisms defines the minor AGXT allele, whereas their absence defines the major allele. The minor allele has frequencies of 20% in normal European and North American populations, and 50% in HP1 patients. The disease is caused by variants affecting the gene represented in this entry. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. The intracellular compartmentalization of AGTX in mammalian hepatocytes is species dependent. In human and rabbit, AGTX is peroxisomal. In new world monkeys (marmoset) and rodents (rat and mouse), it is distributed approximately evenly between peroxisomes and mitochondria. In carnivores, like cat, the great majority of the enzyme is mitochondrial with only a small proportion being peroxisomal.