AGX1/YFL030W Summary Help

AGX1 BASIC INFORMATION

Standard Name AGX1
Systematic Name YFL030W
Feature Type ORF, Verified
Description Alanine:glyoxylate aminotransferase (AGT), catalyzes the synthesis of glycine from glyoxylate, which is one of three pathways for glycine biosynthesis in yeast; has similarity to mammalian and plant alanine:glyoxylate aminotransferases (1 and see Summary Paragraph)
Name Description Alanine:Glyoxylate aminotrans(X)ferase 1
Gene Product Alias alanine:glyoxylate aminotransferase 2
GO Annotations All AGX1 GO evidence and references
    View Computational GO annotations for AGX1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Pathways
Mutant Phenotype All AGX1 Phenotype details and references
Large-scale survey
null
overexpression
Interactions AGX1 All interactions details and references
11 total interaction(s) for 11 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 1
Genetic Interactions
  • Synthetic Lethality: 7
Sequence Information
ChrVI:76829 to 77986 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1158 76829..77986 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000001864

AGX1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for AGX1

SUMMARY PARAGRAPH for AGX1

AGX1 encodes an alanine:glyoxylate aminotransferase (AGT) that catalyzes the transfer of the amino group of L-alanine to glyoxylate to produce pyruvate and glycine (3, 2). Although glycine biosynthesis from L-alanine and glyoxylate is one of three pathways that produce glycine, it is the major pathway when cells are grown on non-fermentable carbon sources and is repressed when cells are grown on glucose (4). Cells disrupted for the other two pathways of glycine biosynthesis (shm1 shm2 gly1 triple mutants) are able to grow on ethanol but require glycine supplementation when grown on glucose (1).

Agx1p has sequence and structural similarity to plant and mammalian AGTs, including the human peroxisomal alanine:glyoxylate aminotransferase (1, 2) which causes primary hyperoxaluria type 1 (OMIM) when mistargeted to the mitochondria. The agx1 mutation is functionally complemented by the human gene, and disease-associated mutations decrease the functionality of the human protein in yeast (5).

Last updated: 2008-09-15

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for AGX1]

1) Schlosser T, et al.  (2004) Alanine: glyoxylate aminotransferase of Saccharomyces cerevisiae-encoding gene AGX1 and metabolic significance. Yeast 21(1):63-73
2) Meyer P, et al.  (2005) Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein. Biochimie 87(12):1041-7
3) Takada Y and Noguchi T  (1985) Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates. Biochem J 231(1):157-63
4) Ulane R and Ogur M  (1972) Genetic and physiological control of serine and glycine biosynthesis in Saccharomyces. J Bacteriol 109(1):34-43
5) Hopper ED, et al.  (2008) In Vivo and in Vitro Examination of Stability of Primary Hyperoxaluria-associated Human Alanine:Glyoxylate Aminotransferase. J Biol Chem 283(45):30493-502