CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028787
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kynureninase 
Protein Synonyms/Alias
 L-kynurenine hydrolase 
Gene Name
 Kynu 
Gene Synonyms/Alias
 mCG_19640 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
39LRLDEEDKLSHFRNCubiquitination[1]
51RNCFYIPKMRDLPSIubiquitination[1]
94YLEEELDKWAKMGAYubiquitination[1]
97EELDKWAKMGAYGHDubiquitination[1]
158KPTPKRHKILLEAKAubiquitination[1]
164HKILLEAKAFPSDHYubiquitination[1]
186LHGLDVEKSMRMVKPubiquitination[1]
320TRFNMDNKLQLIPGAubiquitination[1]
385SKDNTENKGPIVNIIubiquitination[1]
450NSFHDVYKFIRLLTSubiquitination[1]
Reference
 [1] 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
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 (By similarity). 
Sequence Annotation
 REGION 166 169 Pyridoxal phosphate binding (By
 BINDING 138 138 Pyridoxal phosphate; via amide nitrogen
 BINDING 139 139 Pyridoxal phosphate (By similarity).
 BINDING 222 222 Pyridoxal phosphate (By similarity).
 BINDING 251 251 Pyridoxal phosphate (By similarity).
 BINDING 254 254 Pyridoxal phosphate (By similarity).
 BINDING 276 276 Pyridoxal phosphate (By similarity).
 BINDING 306 306 Pyridoxal phosphate (By similarity).
 BINDING 334 334 Pyridoxal phosphate (By similarity).
 MOD_RES 2 2 N-acetylmethionine (By similarity).
 MOD_RES 277 277 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Hydrolase; Pyridine nucleotide biosynthesis; Pyridoxal phosphate; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 465 AA 
Protein Sequence
MMEPSPLELP VDAVRRIAAE LNCDPTDERV ALRLDEEDKL SHFRNCFYIP KMRDLPSIDL 60
SLVSEDDDAI YFLGNSLGLQ PKMVRTYLEE ELDKWAKMGA YGHDVGKRPW IVGDESIVSL 120
MKDIVGAHEK EIALMNALTI NLHLLLLSFF KPTPKRHKIL LEAKAFPSDH YAIESQIQLH 180
GLDVEKSMRM VKPREGEETL RMEDILEVIE EEGDSIAVIL FSGLHFYTGQ LFNIPAITKA 240
GHAKGCFVGF DLAHAVGNVE LRLHDWGVDF ACWCSYKYLN SGAGGLAGAF VHEKHAHTVK 300
PALVGWFGHD LSTRFNMDNK LQLIPGANGF RISNPPILLV CSLHASLEVF QQATMTALRR 360
KSILLTGYLE YMLKHYHSKD NTENKGPIVN IITPSRAEER GCQLTLTFSI PKKSVFKELE 420
KRGVVCDKRE PDGIRVAPVP LYNSFHDVYK FIRLLTSILD SSERS 465 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0030429; F:kynureninase activity; IEA:HAMAP.
 GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
 GO:0043420; P:anthranilate metabolic process; IEA:HAMAP.
 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; IEA:HAMAP.
 GO:0034341; P:response to interferon-gamma; IEA:Compara.
 GO:0034516; P:response to vitamin B6; IEA:Compara.
 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