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AGXT Defects in AGXT are the cause of hyperoxaluria primary type 1 (HP1); also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1 is a rare autosomal recessive inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Note: This description may include information from UniProtKB.
Protein type: Amino Acid Metabolism - alanine, aspartate and glutamate; Amino Acid Metabolism - glycine, serine and threonine; EC; EC; Mitochondrial; Motility/polarity/chemotaxis; Transferase
Chromosomal Location of Human Ortholog: 2q37.3
Cellular Component: intracellular membrane-bound organelle; peroxisomal matrix; peroxisome
Molecular Function: alanine-glyoxylate transaminase activity; amino acid binding; protein binding; protein homodimerization activity; protein self-association; pyridoxal phosphate binding; receptor binding; serine-pyruvate transaminase activity; transaminase activity
Biological Process: glycine biosynthetic process, by transamination of glyoxylate; glyoxylate catabolic process; glyoxylate metabolic process; L-alanine catabolic process; L-cysteine catabolic process
Disease: Hyperoxaluria, Primary, Type I
Reference #:  P21549 (UniProtKB)
Alt. Names/Synonyms: AGT; AGT1; AGXT; AGXT1; Alanine--glyoxylate aminotransferase; alanine-glyoxylate aminotransferase; hepatic peroxisomal alanine:glyoxylate aminotransferase; L-alanine: glyoxylate aminotransferase 1; PH1; Serine--pyruvate aminotransferase; serine-pyruvate aminotransferase; serine:pyruvate aminotransferase; SPAT; SPT; SPYA; TLH6
Gene Symbols: AGXT
Molecular weight: 43,010 Da
Basal Isoelectric point: 8.61  Predict pI for various phosphorylation states
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Protein Structure Not Found.
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