ID KYNU_CAEBR Reviewed; 483 AA. AC A8XKT0; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_03017}; DE EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_03017}; DE AltName: Full=Abnormal fluorescence under UV illumination; DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_03017}; GN Name=flu-2; ORFNames=CBG14833; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R.M., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). CC -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- CC hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- CC hydroxyanthranilic acid (3-OHAA), respectively. {ECO:0000255|HAMAP- CC Rule:MF_03017}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine; CC Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972; EC=3.7.1.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03017}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) + CC L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972, CC ChEBI:CHEBI:58125; EC=3.7.1.3; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03017}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03017}; CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine CC and anthranilate from L-kynurenine: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_03017}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_03017}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03017}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03017}. CC -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000255|HAMAP- CC Rule:MF_03017}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HE600983; CAP33254.1; -; Genomic_DNA. DR RefSeq; XP_002644815.1; XM_002644769.1. DR AlphaFoldDB; A8XKT0; -. DR SMR; A8XKT0; -. DR STRING; 6238.A8XKT0; -. DR EnsemblMetazoa; CBG14833.1; CBG14833.1; WBGene00035224. DR GeneID; 8586811; -. DR KEGG; cbr:CBG_14833; -. DR CTD; 8586811; -. DR WormBase; CBG14833; CBP18263; WBGene00035224; Cbr-flu-2. DR eggNOG; KOG3846; Eukaryota. DR HOGENOM; CLU_003433_4_0_1; -. DR InParanoid; A8XKT0; -. DR OMA; LPGWNSH; -. DR OrthoDB; 5471916at2759; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000008549; Chromosome X. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA. DR GO; GO:0030429; F:kynureninase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule. DR GO; GO:0043420; P:anthranilate metabolic process; IBA:GO_Central. DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_01970; Kynureninase; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR010111; Kynureninase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR01814; kynureninase; 1. DR PANTHER; PTHR14084; KYNURENINASE; 1. DR PANTHER; PTHR14084:SF0; KYNURENINASE; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF038800; KYNU; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; Pyridine nucleotide biosynthesis; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1..483 FT /note="Kynureninase" FT /id="PRO_0000356959" FT BINDING 154 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 155 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 182..185 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 238 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 267 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 270 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 292 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 322 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 350 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT MOD_RES 293 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" SQ SEQUENCE 483 AA; 54408 MW; F7BD3B8CB98C956A CRC64; MAEGQAPAPP QPEGDQECMC TQDKVLQFLN KMADESGIKD LTDPALAEFL TDSDALKGIR DLFHYPKAGT LPDVDPTLVD PNADSIYLCG NSLGLMPKVT EEVMKEHLDK WAKMGVFGHM TGEVPWAHSD EHCLEGVGRL VGAKKEEVSI ANSLTVNIHV LLTAFYKPTE TRHKILLESK AFPSDHYAIE SQIRLKGRTV EESMVCMEPR EGEETLRTED IIDYIENNGD EIAIVFFSGI QYYTGQLFDI KAITEAGHRK GCLVGWDLAH AFANVPLHLH WWDVDFAAWC SYKYGCTGAG SIAGLFVHER FLHDKRDRML GWWSHKMSSR FTMDNVLDLD EGAAGYRISN PPIHCVAAML GSLKIFDQVS LENLRSRSCY LTGYLEYLVK TLFGENSEQR TTKLSILIIT PENFHQRGCQ LSLKFSSPID VIYPELVKRG VAVDKRYPNV IRVAPVHLYN NYVDVRRFIS VLQEVAHIVE DHA //