ID KYNU_XANOP Reviewed; 423 AA. AC B2SIT8; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 90. 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=PXO_00758; OS Xanthomonas oryzae pv. oryzae (strain PXO99A). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=360094; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PXO99A; RX PubMed=18452608; DOI=10.1186/1471-2164-9-204; RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D., RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R., RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A., RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R., RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S., RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E., RA White F.F., Bogdanove A.J.; RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas RT oryzae pv. oryzae PXO99A."; RL BMC Genomics 9:204-204(2008). 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; CP000967; ACD58733.1; -; Genomic_DNA. DR RefSeq; WP_012444804.1; NC_010717.2. DR AlphaFoldDB; B2SIT8; -. DR SMR; B2SIT8; -. DR KEGG; xop:PXO_00758; -. DR eggNOG; COG3844; Bacteria. DR HOGENOM; CLU_003433_4_0_6; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000001740; 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..423 FT /note="Kynureninase" FT /id="PRO_0000357020" 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 273 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 301 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 423 AA; 46115 MW; 4DC67FDCBA30463A CRC64; MTDLLSRAHA DALDAADPLR SLRDAFVFPQ HGDRDQTYLV GNSLGLQPRA ARAMVDEVLD QWGTLGVEGH FTGPTQWLTY HQLVRDALAR VVGAQPGEVV AMNTLSVNLH LMMASFYRPT HERGAILIEA GAFPSDRHAV ESQLRLRGLD PATHLIEVEA DEPNGTLSMA AIADAIAQHG PRLALVLWPG IQYRTGQAFD LAEIVRLARA QGAAVGCDLA HAVGNIPLTL HDDGVDFAVW CNYKYLNAGP GAVGGCFVHE RHANSDLPRI AGWWGHEQQT RFRMDPQFVP SPGAEGWQLS NPPVLALAPL RASLTLFDQA GMAALRAKSE RLTGHLEQLI RARVPQVLQI VTPAEPMRRG CQLSLRVAGG RAQGRSLFEH LHAAGVLGDW REPDVIRIAP VPLYNRFSDL HTFVGQVEAW AAA //