ID KYNU_FLAPJ Reviewed; 425 AA. AC A6H1P7; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_01970}; DE EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_01970}; DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_01970}; GN Name=kynU {ECO:0000255|HAMAP-Rule:MF_01970}; OrderedLocusNames=FP2215; OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 / OS JIP02/86). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=402612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86; RX PubMed=17592475; DOI=10.1038/nbt1313; RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B., RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F., RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.; RT "Complete genome sequence of the fish pathogen Flavobacterium RT psychrophilum."; RL Nat. Biotechnol. 25:763-769(2007). 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_01970}. 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_01970}; 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_01970}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01970}; 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_01970}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01970}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01970}. CC -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000255|HAMAP- CC Rule:MF_01970}. 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; AM398681; CAL44271.1; -; Genomic_DNA. DR RefSeq; WP_011964305.1; NC_009613.3. DR RefSeq; YP_001297072.1; NC_009613.3. DR AlphaFoldDB; A6H1P7; -. DR SMR; A6H1P7; -. DR STRING; 402612.FP2215; -. DR EnsemblBacteria; CAL44271; CAL44271; FP2215. DR GeneID; 66553318; -. DR KEGG; fps:FP2215; -. DR PATRIC; fig|402612.5.peg.2262; -. DR eggNOG; COG3844; Bacteria. DR HOGENOM; CLU_003433_4_0_10; -. DR OrthoDB; 9812626at2; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000006394; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA. DR GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule. 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; IEA:UniProtKB-UniRule. 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:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule. 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 Hydrolase; Pyridine nucleotide biosynthesis; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1..425 FT /note="Kynureninase" FT /id="PRO_0000357006" FT BINDING 105 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 106 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 133..136 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 218 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 221 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 243 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 274 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 302 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT MOD_RES 244 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" SQ SEQUENCE 425 AA; 49035 MW; 43111D4A09B97240 CRC64; MIFQNTLEFA QQLDNQDELK EYKNEFIFPQ HEGKNVIYFT GNSLGLQPKS ARNYVDEVMN DWANLAVEGH FYADKPWWDY QERFANPLSK IVGAKPLEVT VMNTLTVNLH LLMVSFYRPT KKRYKIICEE KAFPSDQYMF QSQVNFHGYK PEDAIVEIKR REGEHNIRLE DILSKIEAVG DELALVLFGG VNYYTGQVFD MKTITEAGHK QGAKVGFDLA HAAGNIKLEL HDWNVDFAAW CSYKYMNSGP GNASGCFVHE KHHSDSNLPR FAGWWGHNKE RRFKMEPTFD PVHGADGWQI SNLPILSLAP YLASVEMFAE VGIEKLIRKR NQITAYLEFI LHEIDKEVKG HFEILTPTNQ EERACQLSVF LHGEGRSLFD YLMKNGVVTD WREPNVIRLA PVPLYCSFED MYNFGQILKK GILEN //