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Protein

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Gene

Aadat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.

Cofactori

Pathwayi: L-lysine degradation via saccharopine pathway

This protein is involved in step 4 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass)
  2. Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass)
  3. no protein annotated in this organism
  4. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Aadat)
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (Dlst)
This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20SubstrateBy similarity1
Binding sitei74SubstrateBy similarity1
Binding sitei202SubstrateBy similarity1
Binding sitei399SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.39. 3474.
2.6.1.7. 3474.
ReactomeiR-MMU-71064. Lysine catabolism.
R-MMU-71240. Tryptophan catabolism.
UniPathwayiUPA00868; UER00838.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Aadat
Synonyms:Kat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1345167. Aadat.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29MitochondrionSequence analysisAdd BLAST29
ChainiPRO_000002060330 – 425Kynurenine/alpha-aminoadipate aminotransferase, mitochondrialAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineCombined sources1
Modified residuei69N6-acetyllysineCombined sources1
Modified residuei172N6-succinyllysineCombined sources1
Modified residuei179N6-acetyllysineCombined sources1
Modified residuei263N6-(pyridoxal phosphate)lysine; alternateBy similarity1
Modified residuei263N6-acetyllysine; alternateCombined sources1
Modified residuei263N6-succinyllysine; alternateCombined sources1
Modified residuei339N6-acetyllysine; alternateCombined sources1
Modified residuei339N6-succinyllysine; alternateCombined sources1
Modified residuei351N6-acetyllysineCombined sources1
Modified residuei367N6-acetyllysine; alternateCombined sources1
Modified residuei367N6-succinyllysine; alternateCombined sources1
Modified residuei422N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9WVM8.
PaxDbiQ9WVM8.
PRIDEiQ9WVM8.

PTM databases

iPTMnetiQ9WVM8.
PhosphoSitePlusiQ9WVM8.

Expressioni

Tissue specificityi

Expressed mainly in kidney and to a lesser amount in liver and brain.1 Publication

Gene expression databases

BgeeiENSMUSG00000057228.
CleanExiMM_AADAT.
ExpressionAtlasiQ9WVM8. baseline and differential.
GenevisibleiQ9WVM8. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9WVM8. 2 interactors.
MINTiMINT-1860782.
STRINGi10090.ENSMUSP00000078436.

Structurei

3D structure databases

ProteinModelPortaliQ9WVM8.
SMRiQ9WVM8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0634. Eukaryota.
COG1167. LUCA.
GeneTreeiENSGT00390000004594.
HOGENOMiHOG000223057.
HOVERGENiHBG050429.
InParanoidiQ9WVM8.
KOiK00825.
OMAiWMKNLQK.
OrthoDBiEOG091G0B8J.
PhylomeDBiQ9WVM8.
TreeFamiTF328598.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WVM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYSRFLTAT SLARKPSPIR TTADILSKAP KTLISLAPGS PNPSMFPFKS
60 70 80 90 100
AAFTVENGST IRFEDDLIKR ALQYSPSYGI PELLSWLKQF QVKLHNPPTV
110 120 130 140 150
NYPPNQGQMD LCITSGCQDG LCKAFEMLIN PGDTILVNEP LFPGTLYAMK
160 170 180 190 200
PLGCNIINVP SDEHGIIPEG LKKILSQWKP EDSKDPTKKT PKFLYTVPNG
210 220 230 240 250
NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFSK PWEPTFLSMD
260 270 280 290 300
VDGRVIRADT FSKTVSSGLR VGFMTGPKTL IQNIVLHTQV SSVHACTLSQ
310 320 330 340 350
LMILQLLHQW GEEGFLAHID RTIDFYKNQR DSILAAADKW LRGLAEWHVP
360 370 380 390 400
KAGMFLWIKV KGISDTKQLI EEKAIEREVL LVPGNGFFID GSAPTSFFRA
410 420
SFSLATPAQM DTAFQRLAQL IKESL
Length:425
Mass (Da):47,598
Last modified:November 1, 1999 - v1
Checksum:iE3A6711CFE96D77E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072376 mRNA. Translation: AAD39680.1.
AK075578 mRNA. Translation: BAC35833.1.
BC012637 mRNA. Translation: AAH12637.1.
CCDSiCCDS22320.1.
RefSeqiNP_035964.1. NM_011834.2.
UniGeneiMm.35020.

Genome annotation databases

EnsembliENSMUST00000079472; ENSMUSP00000078436; ENSMUSG00000057228.
GeneIDi23923.
KEGGimmu:23923.
UCSCiuc009lte.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072376 mRNA. Translation: AAD39680.1.
AK075578 mRNA. Translation: BAC35833.1.
BC012637 mRNA. Translation: AAH12637.1.
CCDSiCCDS22320.1.
RefSeqiNP_035964.1. NM_011834.2.
UniGeneiMm.35020.

3D structure databases

ProteinModelPortaliQ9WVM8.
SMRiQ9WVM8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVM8. 2 interactors.
MINTiMINT-1860782.
STRINGi10090.ENSMUSP00000078436.

PTM databases

iPTMnetiQ9WVM8.
PhosphoSitePlusiQ9WVM8.

Proteomic databases

MaxQBiQ9WVM8.
PaxDbiQ9WVM8.
PRIDEiQ9WVM8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079472; ENSMUSP00000078436; ENSMUSG00000057228.
GeneIDi23923.
KEGGimmu:23923.
UCSCiuc009lte.1. mouse.

Organism-specific databases

CTDi51166.
MGIiMGI:1345167. Aadat.

Phylogenomic databases

eggNOGiKOG0634. Eukaryota.
COG1167. LUCA.
GeneTreeiENSGT00390000004594.
HOGENOMiHOG000223057.
HOVERGENiHBG050429.
InParanoidiQ9WVM8.
KOiK00825.
OMAiWMKNLQK.
OrthoDBiEOG091G0B8J.
PhylomeDBiQ9WVM8.
TreeFamiTF328598.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00838.
BRENDAi2.6.1.39. 3474.
2.6.1.7. 3474.
ReactomeiR-MMU-71064. Lysine catabolism.
R-MMU-71240. Tryptophan catabolism.

Miscellaneous databases

ChiTaRSiAadat. mouse.
PROiQ9WVM8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000057228.
CleanExiMM_AADAT.
ExpressionAtlasiQ9WVM8. baseline and differential.
GenevisibleiQ9WVM8. MM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAADAT_MOUSE
AccessioniPrimary (citable) accession number: Q9WVM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.