CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009997
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kynureninase 
Protein Synonyms/Alias
 L-kynurenine hydrolase 
Gene Name
 Kynu 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
38LRLDEEDKLKRFKDCacetylation[1]
40LDEEDKLKRFKDCFYacetylation[1]
84GLQPKMVKTYLEEELacetylation[1]
121ESIVSLMKDIVGAHEacetylation[1]
157KPTPKRHKILLEAKAacetylation[1]
416ISKKGVFKELEKRGVacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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 (By
 BINDING 137 137 Pyridoxal phosphate; via amide nitrogen
 BINDING 138 138 Pyridoxal phosphate (By similarity).
 BINDING 221 221 Pyridoxal phosphate (By similarity).
 BINDING 250 250 Pyridoxal phosphate (By similarity).
 BINDING 253 253 Pyridoxal phosphate (By similarity).
 BINDING 275 275 Pyridoxal phosphate (By similarity).
 BINDING 305 305 Pyridoxal phosphate (By similarity).
 BINDING 333 333 Pyridoxal phosphate (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 276 276 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Pyridine nucleotide biosynthesis; Pyridoxal phosphate; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 464 AA 
Protein Sequence
MEPSPLELPV DAVRRIATEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK MRDLPSIDLS 60
LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY GHEVGKRPWI IGDESIVSLM 120
KDIVGAHEKE IALMNALTVN LHLLLLSFFK PTPKRHKILL EAKAFPSDHY AIESQIQLHG 180
LDVEKSMRMI KPREGEETLR MEDILEVIEK EGDSIAVVLF SGLHFYTGQL FNIPAITQAG 240
HAKGCFVGFD LAHAVGNVEL HLHDWDVDFA CWCSYKYLNS GAGGLAGAFI HEKHAHTIKP 300
ALVGWFGHEL STRFNMDNKL QLIPGVNGFR ISNPPILLVC SLHASLEIFQ QATMTALRRK 360
SILLTGYLEY LLKHYHGGND TENKRPVVNI ITPSRAEERG CQLTLTFSIS KKGVFKELEK 420
RGVVCDKREP EGIRVAPVPL YNSFHDVYKF IRLLTAILDS TERN 464 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0030429; F:kynureninase activity; IDA:RGD.
 GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
 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; IDA:RGD.
 GO:0019441; P:tryptophan catabolic process to kynurenine; IDA:RGD. 
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