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T. maritima Browser
1vjo
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Protein Summary
Alanine-glyoxylate aminotransferase (AGT) from Anabaena sp. (EC 2.6.1.44; COG0075, Pfam00266) is a pyridoxal-phosphate (PLP) dependent enzyme involved in serine-glycine metabolism, where it catalyses the transamination of L-alanine and glyoxylate to pyruvate and glycine.The protein shows close structural resemblance with the human alanine:glyoxylate aminotransferase. In humans, where AGT is peroxisomal, a single point mutation miss-localizes the protein to the mitochondrion, leading to the hereditary kidney stone disease: primary hyperoxaluria type 1 (PubMed:12686111). AGT peroxisomal or mitochondrial location is species-dependent and related to diet in mammals (PubMed:14739251).
Anabaena AGT forms dimer in crystal structure; where each monomer has fold of PLP-dependent transferases (SCOP sunid: 53382). The main N-terminal domain has 3 layers: ???, mixed ?-sheet of 7 strands, order 3245671; strand 7 is antiparallel to the rest. The C-terminal domain is a 2-layer ?? structure, with the 3-stranded, antiparallel ?-sheet packs against the edge of the N-terminal domain (PubMed:15657930).
Ligand Summary
References
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References
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