Curated summary · agent-written · kb/genes/curated/hgnc_341.md

All 15 claims checked against the KB draft

AGXT across dismech

AGXT (alanine--glyoxylate aminotransferase) is named by 2 disorder entries: Primary Hyperoxaluria Type 1; and Primary Hyperoxaluria Type 3.

Normal function

ai-gene-review gives AGXT's core molecular functions as L-alanine:glyoxylate transaminase activity; and L-serine:pyruvate transaminase activity, acting in L-alanine catabolic process; L-serine catabolic process; glycine biosynthetic process; and glyoxylate catabolic process, located in peroxisomal matrix; and peroxisome. The KB's AGXT nodes share glyoxylate catabolic process with those core functions: the PH1 trigger node marks that process as decreased, the dysfunction counterpart of the transamination of glyoxylate to glycine.

Causative record

One entry types AGXT as causative, Primary Hyperoxaluria Type 1, with the variants recorded as germline. There the gene sits on the node AGXT Alanine-Glyoxylate Aminotransferase Deficiency.

Modifier record

In Primary Hyperoxaluria Type 3 AGXT is typed modifier, from a single family in which a heterozygous AGXT variant accompanied a more severe HOGA1-related phenotype. No pathophysiology node in that entry names AGXT (0).

Where the layers disagree

ClinGen classifies AGXT for 1 disease, and that disease has no dismech entry matched to it: alanine glyoxylate aminotransferase deficiency. That MONDO term is the parent of primary hyperoxaluria type 1, so the ClinGen tier is not attached to the PH1 record.

Underlined values are claims re-computed from the knowledge base each time this page is built. The tables below are the source of truth.

Normal function · from ai-gene-review (P21549, commit 79fe13b38970) · AI-generated, not KB evidence

Human AGXT encodes a liver-enriched, pyridoxal 5'-phosphate (PLP)-dependent aminotransferase that acts as a homodimer in the peroxisomal matrix. It transfers the amino group of L-alanine to glyoxylate, producing pyruvate and glycine and limiting the glyoxylate available for oxalate formation. A second substrate reaction, L-serine:pyruvate transamination, produces hydroxypyruvate and alanine and contributes to serine breakdown in human liver preparations. PEX5 recognizes its C-terminal KKL targeting signal together with contacts in the folded C-terminal domain. Loss of activity, aggregation, or altered intracellular targeting of AGXT causes primary hyperoxaluria type 1.

PLP-dependent, homodimeric alanine:glyoxylate transaminase converts glyoxylate and L-alanine to glycine and pyruvate in the peroxisomal matrix, limiting glyoxylate availability for oxalate formation. Amino-acid substrate binding supplies recognition within this catalytic cycle.

molecular function: L-alanine:glyoxylate transaminase activity · directly involved in: glyoxylate catabolic process; glycine biosynthetic process; L-alanine catabolic process · locations: peroxisomal matrix

PLP-dependent serine:pyruvate transaminase converts L-serine and pyruvate to hydroxypyruvate and L-alanine in liver peroxisomes. This reaction contributes substantially to serine breakdown in human liver preparations under the tested quasi-physiological in-vitro conditions.

molecular function: L-serine:pyruvate transaminase activity · directly involved in: L-serine catabolic process · locations: peroxisome

In the knowledge base · computed from kb/ at build time

Disorders

Relationship is the entry's genetic[].relationship_type. untyped means the entry has a genetic record for the gene but does not type it; its free-text association is shown instead.

Disorder	Relationship	Where the gene appears
Primary Hyperoxaluria Type 1	causative germline	mechanism: AGXT Alanine-Glyoxylate Aminotransferase Deficiency
Primary Hyperoxaluria Type 3	modifier germline

ClinGen gene–disease validity · snapshot 2026-10-03 · matched to entries by MONDO

An entry matches when ClinGen's MONDO disease is the entry's own disease term, a subtype term, or an exact-match mapping. An amber status marks an entry ClinGen supports the gene for (Definitive, Strong or Moderate) whose own record does not type it. A Limited, Disputed or Refuted tier on such an entry is not a gap.

ClinGen disease	MOI	Classification	dismech entry
alanine glyoxylate aminotransferase deficiency MONDO:0100278	AR	Definitive 2020-02-07	no dismech entry