Aadat aminoadipate aminotransferase [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Aadatprovided by RGD
Official Full Name: aminoadipate aminotransferaseprovided by RGD
Primary source: RGD:2948
See related: EnsemblRapid:ENSRNOG00000011861 AllianceGenome:RGD:2948
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: Kat2
Summary: Enables 2-aminoadipate transaminase activity; kynurenine-glyoxylate transaminase activity; and kynurenine-oxoglutarate transaminase activity. Predicted to be involved in 2-oxoglutarate metabolic process; glutamate metabolic process; and kynurenine metabolic process. Predicted to be located in mitochondrion. Orthologous to human AADAT (aminoadipate aminotransferase). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Kidney (RPKM 1947.0) and Liver (RPKM 376.0) See more
Orthologs: human mouse all
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Genomic context

Location:: 16p12

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	16	NC_086034.1 (34520236..34566388, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	16	NC_051351.1 (29509392..29544332, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	16	NC_005115.4 (32832001..32868680, complement)

Chromosome 16 - NC_086034.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

We found specific staining of KAT II-positive astrocyte-like cells throughout the adult rat brain. The presence of KAT II in astrocytes was confirmed by double fluorescence immunostaining with an antibody against the astrocyte-specific marker GFAP.
Title: Astrocytic localization of kynurenine aminotransferase II in the rat brain visualized by immunocytochemistry.
neuronal culture showed positive immunostaining for both kynurenic acid aminotransferase (KAT) isoforms I and II
Title: Demonstration of kynurenine aminotransferases I and II and characterization of kynurenic acid synthesis in cultured cerebral cortical neurons.
identification of presence in the permanent immature rat oligodendrocyte cell line OLN-93
Title: Demonstration of kynurenine aminotransferases I and II and characterization of kynurenic acid synthesis in oligodendrocyte cell line (OLN-93).

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General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables 2-aminoadipate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables 2-aminoadipate transaminase activity	IEA Inferred from Electronic Annotation more info
enables 2-aminoadipate transaminase activity	ISO Inferred from Sequence Orthology more info
enables 2-aminoadipate transaminase activity	ISS Inferred from Sequence or Structural Similarity more info
enables glycine:2-oxoglutarate aminotransferase activity	IEA Inferred from Electronic Annotation more info
enables glycine:2-oxoglutarate aminotransferase activity	ISO Inferred from Sequence Orthology more info
enables glycine:2-oxoglutarate aminotransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables kynurenine-glyoxylate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables kynurenine-glyoxylate transaminase activity	IEA Inferred from Electronic Annotation more info
enables kynurenine-glyoxylate transaminase activity	ISO Inferred from Sequence Orthology more info
enables kynurenine-glyoxylate transaminase activity	ISS Inferred from Sequence or Structural Similarity more info
enables kynurenine-oxoglutarate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables kynurenine-oxoglutarate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables kynurenine-oxoglutarate transaminase activity	IEA Inferred from Electronic Annotation more info
enables kynurenine-oxoglutarate transaminase activity	ISO Inferred from Sequence Orthology more info
enables kynurenine-oxoglutarate transaminase activity	ISS Inferred from Sequence or Structural Similarity more info
enables methionine-glyoxylate transaminase activity	IEA Inferred from Electronic Annotation more info
enables methionine-glyoxylate transaminase activity	ISO Inferred from Sequence Orthology more info
enables methionine-glyoxylate transaminase activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein homodimerization activity	IEA Inferred from Electronic Annotation more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables pyridoxal phosphate binding	IEA Inferred from Electronic Annotation more info
enables transaminase activity	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in 2-oxoglutarate metabolic process	IEA Inferred from Electronic Annotation more info
involved_in 2-oxoglutarate metabolic process	ISO Inferred from Sequence Orthology more info
involved_in 2-oxoglutarate metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in L-lysine catabolic process to acetyl-CoA via saccharopine	IEA Inferred from Electronic Annotation more info
involved_in alpha-amino acid metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in glutamate metabolic process	IEA Inferred from Electronic Annotation more info
involved_in glutamate metabolic process	ISO Inferred from Sequence Orthology more info
involved_in glutamate metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in kynurenine metabolic process	IEA Inferred from Electronic Annotation more info
involved_in kynurenine metabolic process	ISO Inferred from Sequence Orthology more info
involved_in kynurenine metabolic process	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
is_active_in cytosol	IDA Inferred from Direct Assay more info	PubMed
is_active_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	ISO Inferred from Sequence Orthology more info	PubMed

General protein information

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Preferred Names: kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Names: 2-aminoadipate aminotransferase; 2-aminoadipate transaminase; KAT/AadAT; alpha-aminoadipate aminotransferase; glycine transaminase AADAT; kynurenine aminotransferase 2; kynurenine aminotransferase II; kynurenine--glyoxylate transaminase AADAT; kynurenine--oxoglutarate aminotransferase II; kynurenine--oxoglutarate transaminase 2; kynurenine--oxoglutarate transaminase II; methionine--glyoxylate transaminase AADAT

NP_058889.1

EC 2.6.1.39

EC 2.6.1.4

EC 2.6.1.63

EC 2.6.1.7

EC 2.6.1.73

XP_063131340.1

EC 2.6.1.39

EC 2.6.1.4

EC 2.6.1.63

EC 2.6.1.7

EC 2.6.1.73

XP_063131341.1

EC 2.6.1.39

EC 2.6.1.4

EC 2.6.1.63

EC 2.6.1.7

EC 2.6.1.73

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_017193.1 → NP_058889.1 kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

See identical proteins and their annotated locations for NP_058889.1

Status: PROVISIONAL

Source sequence(s)

Z50144

UniProtKB/Swiss-Prot

Q64602

UniProtKB/TrEMBL

A0A8L2Q812, A6KIT5

Related

ENSRNOP00000015974.5, ENSRNOT00000015974.7

Conserved Domains (1) summary

COG1167
Location:20 → 423

ARO8; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]