CPLM-015479

Genbank Nucleotide ID

Kynurenine--oxoglutarate transaminase 3

Protein Synonyms/Alias

Cysteine-S-conjugate beta-lyase 2; Kynurenine aminotransferase III; KATIII; Kynurenine--glyoxylate transaminase; Kynurenine--oxoglutarate transaminase III

Homo sapiens (Human)

Position	Peptide	Type	References
82	ISPPTYVKEELSKIA	ubiquitination	[1, 2]
87	YVKEELSKIAAIDSL	ubiquitination	[1]
108	FGHPSLVKALSYLYE	acetylation	[3]
108	FGHPSLVKALSYLYE	ubiquitination	[4]
116	ALSYLYEKLYQKQID	acetylation	[3]
120	LYEKLYQKQIDSNKE	ubiquitination	[1]
203	DPQELESKFNSKTKA	ubiquitination	[1, 5]
222	TPHNPLGKVYNREEL	ubiquitination	[1]
396	NNEPYDYKFVKWMTK	ubiquitination	[1]
399	PYDYKFVKWMTKHKK	ubiquitination	[5]
421	AFCNSETKSQFEKFV	ubiquitination	[5]
434	FVRFCFIKKDSTLDA	ubiquitination	[5]
447	DAAEEIIKAWSVQKS	ubiquitination	[1, 4, 5]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]

Functional Description

Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se- conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2- oxoglutarate as amino group acceptor (in vitro) (By similarity).

BINDING 53 53 Substrate (By similarity).
BINDING 71 71 Substrate; via amide nitrogen (By
BINDING 218 218 Substrate (By similarity).
BINDING 429 429 Substrate (By similarity).
MOD_RES 116 116 N6-acetyllysine.
MOD_RES 280 280 N6-(pyridoxal phosphate)lysine (By

Acetylation; Alternative splicing; Aminotransferase; Complete proteome; Lyase; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005739; C:mitochondrion; IEA:Compara.
GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:EC.
GO:0047315; F:kynurenine-glyoxylate transaminase activity; ISS:UniProtKB.
GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO:0006103; P:2-oxoglutarate metabolic process; IEA:Compara.
GO:0009058; P:biosynthetic process; IEA:InterPro.
GO:0006569; P:tryptophan catabolic process; TAS:Reactome.

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

PF00155; Aminotran_1_2