Agxt alanine--glyoxylate aminotransferase [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Agxtprovided by RGD
Official Full Name: alanine--glyoxylate aminotransferaseprovided by RGD
Primary source: RGD:2073
See related: Ensembl:ENSRNOG00000023856 AllianceGenome:RGD:2073
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: AGT; SPT; Spat
Summary: This gene encodes alanine-glyoxylate aminotransferase, which catalyzes the interconversion of L-alanine and glyoxylate to pyruvate and glycine. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. The longer transcript variant includes an upstream translation start codon and a downstream translation start codon. The upstream start codon initiates the translation of the mitochondrial enzyme precursor while the downstream start codon initiates the translation of the peroxisomal enzyme (see PMID:2332438). [provided by RefSeq, Feb 2013]
Expression: Restricted expression toward (RPKM 541.7) See more
Orthologs: human mouse all
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Genomic context

Location:: 9q36

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	9	NC_086027.1 (101122793..101132746)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	9	NC_051344.1 (93675384..93685337)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	9	NC_005108.4 (100281339..100291292)

Chromosome 9 - NC_086027.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

biochemical analyses have allowed elucidation of the mechanism of action of AGT (alanine:glyoxylate aminotransferase) and the way in which the disease causing G82E mutation affects it
Title: Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications.
serine:pyruvate aminotransferase expression is regulated by Sp1, AP-2 and PKA
Title: The role of Sp1 and AP-2 in basal and protein kinase A--induced expression of mitochondrial serine:pyruvate aminotransferase in hepatocytes.

Submit: New GeneRIF Correction

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables alanine-glyoxylate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables alanine-glyoxylate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables alanine-glyoxylate transaminase activity	ISO Inferred from Sequence Orthology more info
enables amino acid binding	IDA Inferred from Direct Assay more info	PubMed
enables amino acid binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISS Inferred from Sequence or Structural Similarity more info
enables pyridoxal phosphate binding	ISO Inferred from Sequence Orthology more info
enables serine-pyruvate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-pyruvate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables serine-pyruvate transaminase activity	ISO Inferred from Sequence Orthology more info
enables transaminase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in L-alanine catabolic process	ISO Inferred from Sequence Orthology more info
involved_in L-cysteine catabolic process	ISO Inferred from Sequence Orthology more info
involved_in L-serine metabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within Notch signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in glycine biosynthetic process, by transamination of glyoxylate	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycine biosynthetic process, by transamination of glyoxylate	IDA Inferred from Direct Assay more info	PubMed
involved_in glycine biosynthetic process, by transamination of glyoxylate	ISO Inferred from Sequence Orthology more info
involved_in glyoxylate catabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within glyoxylate metabolic process	ISO Inferred from Sequence Orthology more info
involved_in glyoxylate metabolic process	ISO Inferred from Sequence Orthology more info
involved_in glyoxylate metabolic process	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within oxalic acid secretion	ISO Inferred from Sequence Orthology more info
involved_in pyruvate biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in response to cAMP	IDA Inferred from Direct Assay more info	PubMed
involved_in response to glucocorticoid	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in intracellular membrane-bounded organelle	ISO Inferred from Sequence Orthology more info
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	TAS Traceable Author Statement more info	PubMed
located_in peroxisomal matrix	ISO Inferred from Sequence Orthology more info
is_active_in peroxisome	IBA Inferred from Biological aspect of Ancestor more info
located_in peroxisome	IDA Inferred from Direct Assay more info	PubMed
located_in peroxisome	ISO Inferred from Sequence Orthology more info
located_in peroxisome	TAS Traceable Author Statement more info	PubMed

General protein information

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Preferred Names: alanine--glyoxylate aminotransferase; serine--pyruvate aminotransferase; serine--pyruvate aminotransferase, peroxisomal

Names: alanine--glyoxylate and serine--pyruvate aminotransferase; angiotensin receptor 2; serine--pyruvate aminotransferase, mitochondrial; serine-pyruvate aminotransferase; serine:pyruvate aminotransferase SPT; serine:pyruvate/alanine:glyoxylate aminotransferase

NP_001257588.1

EC 2.6.1.44

EC 2.6.1.51

NP_001263635.1

EC 2.6.1.44

EC 2.6.1.51

NP_085914.2

EC 2.6.1.44

EC 2.6.1.51

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001270659.1 → NP_001257588.1 serine--pyruvate aminotransferase isoform 2

Status: REVIEWED

Description

Transcript Variant: This variant (2) has multiple differences, compared to variant 1. The resulting isoform (2) is much shorter and has a distinct N-terminus, compared to isoform 1. The cellular location of isoform 2 is not determined.

Source sequence(s)

AI029012, FQ228944

UniProtKB/TrEMBL

A0A0G2JYE8

Related

ENSRNOP00000070626.1, ENSRNOT00000079305.2

Conserved Domains (2) summary

COG0075
Location:56 → 179

PucG; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]

cl18945
Location:56 → 180

AAT_I; Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the ...
NM_001276706.1 → NP_001263635.1 serine--pyruvate aminotransferase, peroxisomal isoform 3

See identical proteins and their annotated locations for NP_001263635.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longer transcript. It contains an upstream start codon and a downstream start codon. Isoform 3, also known as the peroxisomal enzyme, is encoded from the downstream start codon, which is identical to the mature peptide of isoform 1, also known as the mitochondrial enzyme.

Source sequence(s)

BC088133, M35270

UniProtKB/TrEMBL

Q5I0N5

Conserved Domains (2) summary

cd06451
Location:24 → 385

AGAT_like; Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), ...

COG0075
Location:21 → 384

PucG; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]
NM_030656.2 → NP_085914.2 alanine--glyoxylate aminotransferase isoform 1 precursor

See identical proteins and their annotated locations for NP_085914.2

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longer transcript. It contains an upstream start codon and a downstream start codon. The upstream start codon initiates the translation of the longest isoform (1), which is a mitochondrial enzyme precursor. The mature peptide, also known as the mitochondrial enzyme, is identical to isoform 3, also known as the peroxisomal enzyme.

Source sequence(s)

BC088133, M35270

UniProtKB/Swiss-Prot

P09139, Q9R2C7

UniProtKB/TrEMBL

A6JQX5, Q5I0N5

Related

ENSRNOP00000030340.2, ENSRNOT00000029127.4

Conserved Domains (2) summary

cd06451
Location:46 → 407

AGAT_like; Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), ...

COG0075
Location:43 → 406

PucG; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]