ID KYNU_CHRFK Reviewed; 425 AA. AC A0M4Y1; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 96. 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}; GN OrderedLocusNames=GFO_2720; OS Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803) OS (Gramella forsetii). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Christiangramia. OX NCBI_TaxID=411154; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17595 / CGMCC 1.15422 / KT0803; RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x; RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., RA Gloeckner F.O.; RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' RT reveals adaptations to degradation of polymeric organic matter."; RL Environ. Microbiol. 8:2201-2213(2006). 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; CU207366; CAL67676.1; -; Genomic_DNA. DR RefSeq; WP_011710579.1; NC_008571.1. DR AlphaFoldDB; A0M4Y1; -. DR SMR; A0M4Y1; -. DR STRING; 411154.GFO_2720; -. DR KEGG; gfo:GFO_2720; -. DR eggNOG; COG3844; Bacteria. DR HOGENOM; CLU_003433_4_0_10; -. DR OrthoDB; 9812626at2; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000000755; 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. FT CHAIN 1..425 FT /note="Kynureninase" FT /id="PRO_0000357008" 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; 49068 MW; 15B0BFA75F3E2AD1 CRC64; MQFENTREFA KKLDNEDKIS KYRDEFIFPK VNGKDVIYFV GNSLGLQPKT ARKYVDEVMK DWAELAVEGH FYAEKSWWDY HERFSEKLAR VVGANPSEVT VMNTLTVNLH LLMVSFYRPS GKRYKIICEE KAFPSDQYMI SSQVRFHGYE PSDAIVEIMK REGENNFRTE DILKKIEEVG EECALVLIGG VNYYTGQVFD METITKAGHD IGAFVGWDLA HGAGNIELKL SEWNVDFAAW CSYKYMNSGP GNASGCFINK KYHNKKDIPR FEGWWGHNKE RRFLMEPEFQ PEPTADAWQI SNAPILALAP YLASLEMFDE VGMPALIEKR NKIVAYLEFV LHEIDEEVDS SFEIITPADQ NERGTQLSVF LHGEGKELFR YLMDQGVITD WREPNVIRLA PAPFYCSFED MYEFGQILKK GILSK //