UniProt Accession

 KYNU_HUMAN; Q16719; B2RCZ5; D3DP79; Q6I9T2; Q9BVW3 

Genbank Protein ID

 U57721; AK315343; CR457423; AC013437; AC013444; CH471058; CH471058; CH471058; BC000879 

Genbank Nucleotide ID

 AAC50650.1; BAG37742.1; CAG33704.1; EAX11599.1; EAX11600.1; EAX11601.1; AAH00879.1 

Protein Name

 Kynureninase 

Protein Synonyms/Alias

 L-kynurenine hydrolase 

Gene Name

 KYNU 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
21	QRIAAELKCHPTDER	ubiquitination	[1]
96	EELDKWAKIAAYGHE	ubiquitination	[2, 3]
163	YKILLEAKAFPSDHY	ubiquitination	[4]
385	KDKAATKKPVVNIIT	ubiquitination	[4]
464	ILDSAETKN******	ubiquitination	[1, 4]

Reference

 [1] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [2] 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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional Description

 Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. 

Sequence Annotation

 REGION 165 168 Pyridoxal phosphate binding.
 BINDING 137 137 Pyridoxal phosphate; via amide nitrogen
 BINDING 138 138 Pyridoxal phosphate.
 BINDING 221 221 Pyridoxal phosphate (By similarity).
 BINDING 250 250 Pyridoxal phosphate.
 BINDING 253 253 Pyridoxal phosphate.
 BINDING 275 275 Pyridoxal phosphate.
 BINDING 305 305 Pyridoxal phosphate.
 BINDING 333 333 Pyridoxal phosphate.
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 276 276 N6-(pyridoxal phosphate)lysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Disease mutation; Hydrolase; Polymorphism; Pyridine nucleotide biosynthesis; Pyridoxal phosphate; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 465 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0030429; F:kynureninase activity; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
 GO:0043420; P:anthranilate metabolic process; IDA:UniProtKB.
 GO:0034354; P:de novo NAD biosynthetic process from tryptophan; IEA:HAMAP.
 GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
 GO:0019805; P:quinolinate biosynthetic process; IDA:UniProtKB.
 GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
 GO:0034516; P:response to vitamin B6; IMP:UniProtKB.
 GO:0006569; P:tryptophan catabolic process; IMP:UniProtKB.
 GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IEA:Compara.
 GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:Compara. 

Interpro

 IPR000192; Aminotrans_V/Cys_dSase.
 IPR010111; Kynureninase.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 

Pfam

 PF00266; Aminotran_5 

SMART

  

PROSITE

  

PRINTS