Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial precursor

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Q9WVM8 (AADAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Short name=KAT/AadAT

Alternative name(s):
2-aminoadipate aminotransferase
2-aminoadipate transaminase
EC=2.6.1.39
Alpha-aminoadipate aminotransferase
Short name=AadAT
Kynurenine aminotransferase II
Kynurenine--oxoglutarate aminotransferase II
Kynurenine--oxoglutarate transaminase 2
EC=2.6.1.7
Kynurenine--oxoglutarate transaminase II

Gene names

Name:	Aadat
Synonyms:	Kat2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) By similarity.
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion Potential.
Tissue specificity	Expressed mainly in kidney and to a lesser amount in liver and brain. Ref.1
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway biosynthetic process Inferred from electronic annotation. Source: InterPro glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB tryptophan catabolic process to kynurenine Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrion Inferred from direct assay PubMed 14651853 PubMed 18614015. Source: MGI
Molecular_function	2-aminoadipate transaminase activity Inferred from sequence or structural similarity. Source: UniProtKB kynurenine-oxoglutarate transaminase activity Inferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

Mitochondrion Potential

Chain

30 – 425

396

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

PRO_0000020603

Sites

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

202

Substrate By similarity

Binding site

399

Substrate By similarity

Amino acid modifications

Modified residue

263

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WVM8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E3A6711CFE96D77E
Show »

FASTA

425

47,598

        10         20         30         40         50         60 
MNYSRFLTAT SLARKPSPIR TTADILSKAP KTLISLAPGS PNPSMFPFKS AAFTVENGST 

        70         80         90        100        110        120 
IRFEDDLIKR ALQYSPSYGI PELLSWLKQF QVKLHNPPTV NYPPNQGQMD LCITSGCQDG 

       130        140        150        160        170        180 
LCKAFEMLIN PGDTILVNEP LFPGTLYAMK PLGCNIINVP SDEHGIIPEG LKKILSQWKP 

       190        200        210        220        230        240 
EDSKDPTKKT PKFLYTVPNG NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFSK 

       250        260        270        280        290        300 
PWEPTFLSMD VDGRVIRADT FSKTVSSGLR VGFMTGPKTL IQNIVLHTQV SSVHACTLSQ 

       310        320        330        340        350        360 
LMILQLLHQW GEEGFLAHID RTIDFYKNQR DSILAAADKW LRGLAEWHVP KAGMFLWIKV 

       370        380        390        400        410        420 
KGISDTKQLI EEKAIEREVL LVPGNGFFID GSAPTSFFRA SFSLATPAQM DTAFQRLAQL 


IKESL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization and expression analysis of mouse kynurenine aminotransferase II, a possible factor in the pathophysiology of Huntington's disease." Yu P., Mosbrook D.M., Tagle D.A. Mamm. Genome 10:845-852(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: 129/SvJ.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF072376 mRNA. Translation: AAD39680.1. AK075578 mRNA. Translation: BAC35833.1. BC012637 mRNA. Translation: AAH12637.1.
IPI	IPI00762346.
RefSeq	NP_035964.1. NM_011834.2.
UniGene	Mm.35020.
3D structure databases
ProteinModelPortal	Q9WVM8.
SMR	Q9WVM8. Positions 1-425.
ModBase	Search...
PTM databases
PhosphoSite	Q9WVM8.
Proteomic databases
PaxDb	Q9WVM8.
PRIDE	Q9WVM8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000079472; ENSMUSP00000078436; ENSMUSG00000057228.
GeneID	23923.
KEGG	mmu:23923.
UCSC	uc009lte.1. mouse.
Organism-specific databases
CTD	51166.
MGI	MGI:1345167. Aadat.
Phylogenomic databases
eggNOG	COG1167.
GeneTree	ENSGT00390000004594.
HOGENOM	HOG000223057.
HOVERGEN	HBG050429.
KO	K00825.
OMA	PFQSASI.
OrthoDB	EOG480HWQ.
Enzyme and pathway databases
UniPathway	UPA00868; UER00838.
Gene expression databases
Bgee	Q9WVM8.
CleanEx	MM_AADAT.
Genevestigator	Q9WVM8.
GermOnline	ENSMUSG00000057228. Mus musculus.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	AADAT. mouse.
NextBio	303709.
SOURCE	Search...

Entry information

Entry name

AADAT_MOUSE

Accession

Primary (citable) accession number: Q9WVM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents