ID KYNU_BURM7 Reviewed; 416 AA. AC A3MHE2; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 99. 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=BMA10247_0099; OS Burkholderia mallei (strain NCTC 10247). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10247; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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=L-kynurenine + H2O = anthranilate + L-alanine + H(+); 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 + L- CC alanine + H(+); 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; CP000548; ABO07333.1; -; Genomic_DNA. DR RefSeq; WP_004189663.1; NC_009080.1. DR AlphaFoldDB; A3MHE2; -. DR SMR; A3MHE2; -. DR GeneID; 92978122; -. DR KEGG; bmaz:BM44_2877; -. DR KEGG; bmn:BMA10247_0099; -. DR PATRIC; fig|320389.8.peg.3247; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0006569; P:L-tryptophan catabolic process; IEA:InterPro. DR GO; GO:0009435; P:NAD+ biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.640.10:FF:000107; Kynureninase; 1. 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; 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; PF22580; KYNU_C; 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..416 FT /note="Kynureninase" FT /id="PRO_0000356995" FT BINDING 97 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 98 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 129..132 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 172 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 201 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 204 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 226 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 256 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 282 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT MOD_RES 227 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" SQ SEQUENCE 416 AA; 45922 MW; 35E6734AC426EE17 CRC64; MKTREEALAL DRDDPLAPLR EQFALPAGVI YLDGNSLGAQ PRAAAARAQQ VIGAEWGEGL IRSWNTAGWF ALPRRLGDRL APLIGAADDE VAITDTISIN LFKLLAAMLR HQARHAPKRR VIVSERSNFP TDLYIAQGLI AQLDRDYELR LIDDPADLPD ALDDETAVAM ITHVNYRTGY MHDMPSVTQT VRQAGALMLW DLAHSAGAVP VDLNGALADG AVGCTYKYLN GGPGSPAFVW VPKRHQRAFE QPLSGWWGHR APFAMQPAFE PDPGIARFLC GTQPIVSMSM VECGLDVFAQ TDMHAIRRKS LALTDAFVAL VESRCAGQPL KLVTPRAHHQ RGSQASFEHP HGYEVMQALI ARGVIGDYRE PRILRFGFTP LYTRFVDVWD AVETLRDILD TEAWRAPEFA TRAAVT //