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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201SubstrateBy similarity
Binding sitei74 – 741SubstrateBy similarity
Binding sitei202 – 2021SubstrateBy similarity
Binding sitei399 – 3991SubstrateBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionSequence analysisAdd
BLAST
Chaini30 – 425396Kynurenine/alpha-aminoadipate aminotransferase, mitochondrialPRO_0000020603Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei69 – 691N6-acetyllysineCombined sources
Modified residuei172 – 1721N6-succinyllysineCombined sources
Modified residuei179 – 1791N6-acetyllysineCombined sources
Modified residuei263 – 2631N6-(pyridoxal phosphate)lysine; alternateBy similarity
Modified residuei263 – 2631N6-acetyllysine; alternateCombined sources
Modified residuei263 – 2631N6-succinyllysine; alternateCombined sources
Modified residuei339 – 3391N6-acetyllysine; alternateCombined sources
Modified residuei339 – 3391N6-succinyllysine; alternateCombined sources
Modified residuei351 – 3511N6-acetyllysineCombined sources
Modified residuei367 – 3671N6-acetyllysine; alternateCombined sources
Modified residuei367 – 3671N6-succinyllysine; alternateCombined sources
Modified residuei422 – 4221N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9WVM8.
MaxQBiQ9WVM8.
PaxDbiQ9WVM8.
PRIDEiQ9WVM8.

PTM databases

iPTMnetiQ9WVM8.
PhosphoSiteiQ9WVM8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9WVM8.
CleanExiMM_AADAT.
GenevisibleiQ9WVM8. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9WVM8.
SMRiQ9WVM8. Positions 1-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0634. Eukaryota.
COG1167. LUCA.
GeneTreeiENSGT00390000004594.
HOGENOMiHOG000223057.
HOVERGENiHBG050429.
InParanoidiQ9WVM8.
KOiK00825.
OMAiPTYYEIP.
OrthoDBiEOG7ZKSBF.
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. Positions 1-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9WVM8.
PhosphoSiteiQ9WVM8.

Proteomic databases

EPDiQ9WVM8.
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.
OMAiPTYYEIP.
OrthoDBiEOG7ZKSBF.
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.
NextBioi303709.
PROiQ9WVM8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVM8.
CleanExiMM_AADAT.
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...

Publicationsi

« Hide 'large scale' publications
  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.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-263; LYS-339 AND LYS-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-179; LYS-263; LYS-339; LYS-351; LYS-367 AND LYS-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: March 16, 2016
This is version 108 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.