ID KYNU_SCLS1 Reviewed; 475 AA. AC A7ESB8; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, 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=Biosynthesis of nicotinic acid protein 5 {ECO:0000255|HAMAP-Rule:MF_03017}; DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_03017}; GN Name=bna5; ORFNames=SS1G_08223; OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) OS (Whetzelinia sclerotiorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Sclerotinia. OX NCBI_TaxID=665079; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18683 / 1980 / Ss-1; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). 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; CH476631; EDN92360.1; -; Genomic_DNA. DR RefSeq; XP_001590483.1; XM_001590433.1. DR AlphaFoldDB; A7ESB8; -. DR SMR; A7ESB8; -. DR STRING; 665079.A7ESB8; -. DR EnsemblFungi; EDN92360; EDN92360; SS1G_08223. DR GeneID; 5486837; -. DR KEGG; ssl:SS1G_08223; -. DR VEuPathDB; FungiDB:sscle_10g075610; -. DR eggNOG; KOG3846; Eukaryota. DR HOGENOM; CLU_003433_4_0_1; -. DR InParanoid; A7ESB8; -. DR OMA; SHVAYRS; -. DR OrthoDB; 5471916at2759; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000001312; Unassembled WGS sequence. 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:SF2; KYNURENINASE 2; 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..475 FT /note="Kynureninase" FT /id="PRO_0000360872" FT BINDING 141 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 142 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 169..172 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 254 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 257 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 279 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 319 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 347 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT MOD_RES 280 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" SQ SEQUENCE 475 AA; 52956 MW; DC42B2E8ED59B7C4 CRC64; MGSIAKEEQP SKVEKPTFSS KANTLEYAQS LDANDHMRRF RDQFIIPSKA NIKATKLEKP GLSDESSIYF CGNSLGLQPK CVKEYLQAHL DTWSSIGVHG HFRDLEDSPL TQWQLLAEHA SKQCAPIVGA KASEVAMMGT LTTNLHLLMA SFYTPTPEKN KIIMEWKAFP SDHYAIESQI RGHGYNPQEA MVMIGPEEGS YEISTEKILR TIDEHASTTA LVLLPGIQYY TGQLFDVKTI TAYAQSKGLI VGWDLAHAAG NVPLQLHDWN VDFAVWCTYK YMNAGPGSIA GAFIHERHGE VDYSEGEEKP KYRHRLMGWY GGDQSCRFLM NNKFRPSPGA SGYQVSNPSV VDLTSLCAAL SIFNQTSMEE ISQKTLHLTA YLEHLLLTSN PSNTNPAFRI ITPSDPSARG TQLSVLLKPG RLETLSDMLE EAGIVADKRK PDVIRVAPVP LYNTYEDVWR FVQIFNAALE KCEEA //