UniProt Accession

 AADAT_MOUSE; Q9WVM8 

Genbank Protein ID

 AF072376; AK075578; BC012637 

Genbank Nucleotide ID

 AAD39680.1; BAC35833.1; AAH12637.1 

Protein Name

 Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial 

Protein Synonyms/Alias

 KAT/AadAT; 2-aminoadipate aminotransferase; 2-aminoadipate transaminase; Alpha-aminoadipate aminotransferase; AadAT; Kynurenine aminotransferase II; Kynurenine--oxoglutarate aminotransferase II; Kynurenine--oxoglutarate transaminase 2; Kynurenine--oxoglutarate transaminase II 

Gene Name

 Aadat 

Gene Synonyms/Alias

 Kat2 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
28	TTADILSKAPKTLIS	acetylation	[1, 2, 3]
28	TTADILSKAPKTLIS	succinylation	[3]
28	TTADILSKAPKTLIS	ubiquitination	[4]
69	RFEDDLIKRALQYSP	acetylation	[1, 2, 3, 5, 6, 7]
69	RFEDDLIKRALQYSP	succinylation	[3]
69	RFEDDLIKRALQYSP	ubiquitination	[4]
172	GIIPEGLKKILSQWK	acetylation	[3]
172	GIIPEGLKKILSQWK	succinylation	[3]
173	IIPEGLKKILSQWKP	acetylation	[1]
179	KKILSQWKPEDSKDP	acetylation	[1, 2, 3, 7]
179	KKILSQWKPEDSKDP	succinylation	[3]
184	QWKPEDSKDPTKKTP	acetylation	[1, 7]
188	EDSKDPTKKTPKFLY	acetylation	[1]
213	NSLTGDRKKEIYELA	ubiquitination	[4]
214	SLTGDRKKEIYELAR	ubiquitination	[4]
263	IRADTFSKTVSSGLR	acetylation	[1, 2, 3, 6, 7, 8]
263	IRADTFSKTVSSGLR	succinylation	[3]
263	IRADTFSKTVSSGLR	ubiquitination	[4]
327	DRTIDFYKNQRDSIL	acetylation	[3, 7]
327	DRTIDFYKNQRDSIL	succinylation	[3]
327	DRTIDFYKNQRDSIL	ubiquitination	[4]
339	SILAAADKWLRGLAE	acetylation	[2, 3, 5, 7]
339	SILAAADKWLRGLAE	succinylation	[3]
339	SILAAADKWLRGLAE	ubiquitination	[4]
351	LAEWHVPKAGMFLWI	acetylation	[2]
367	VKGISDTKQLIEEKA	acetylation	[1, 2, 3, 7]
367	VKGISDTKQLIEEKA	succinylation	[3]
367	VKGISDTKQLIEEKA	ubiquitination	[4]
373	TKQLIEEKAIEREVL	acetylation	[1, 2]
373	TKQLIEEKAIEREVL	ubiquitination	[4]
422	QRLAQLIKESL****	acetylation	[2, 7]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [8] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199] 

Functional Description

 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). 

Sequence Annotation

 BINDING 20 20 Substrate (By similarity).
 BINDING 74 74 Substrate (By similarity).
 BINDING 202 202 Substrate (By similarity).
 BINDING 399 399 Substrate (By similarity).
 MOD_RES 263 263 N6-(pyridoxal phosphate)lysine (By  

Keyword

 Aminotransferase; Complete proteome; Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 425 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0047536; F:2-aminoadipate transaminase activity; ISS:UniProtKB.
 GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:Compara.
 GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
 GO:0009058; P:biosynthetic process; IEA:InterPro.
 GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
 GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
 GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:Compara. 

Interpro

 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 

Pfam

 PF00155; Aminotran_1_2 

SMART

  

PROSITE

  

PRINTS