ID KYNU_PSEFL Reviewed; 416 AA. AC P83788; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2004, sequence version 1. DT 13-SEP-2023, entry version 76. 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}; OS Pseudomonas fluorescens. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294; RN [1] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, RP CATALYTIC ACTIVITY, HOMODIMERIZATION, AND MUTAGENESIS OF ASP-132 AND RP ASP-201. RX PubMed=14756555; DOI=10.1021/bi035744e; RA Momany C., Levdikov V., Blagova L., Lima S., Phillips R.S.; RT "Three-dimensional structure of kynureninase from Pseudomonas RT fluorescens."; RL Biochemistry 43:1193-1203(2004). 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. 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 ECO:0000269|PubMed:14756555}; 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, ECO:0000269|PubMed:14756555}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; 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 ECO:0000269|PubMed:14756555}. 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 PDB; 1QZ9; X-ray; 1.85 A; A=1-416. DR PDBsum; 1QZ9; -. DR AlphaFoldDB; P83788; -. DR SMR; P83788; -. DR DrugBank; DB02343; 3,6,9,12,15-Pentaoxaheptadecane. DR BioCyc; MetaCyc:MONOMER-7065; -. DR BRENDA; 3.7.1.3; 5121. DR SABIO-RK; P83788; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR EvolutionaryTrace; P83788; -. 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Pyridine nucleotide biosynthesis; KW Pyridoxal phosphate. FT CHAIN 1..416 FT /note="Kynureninase" FT /id="PRO_0000357010" FT BINDING 97 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970, FT ECO:0000269|PubMed:14756555" FT BINDING 98 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970, FT ECO:0000269|PubMed:14756555" FT BINDING 129..132 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT BINDING 172 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970, FT ECO:0000269|PubMed:14756555" FT BINDING 201 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970, FT ECO:0000269|PubMed:14756555" FT BINDING 204 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970, FT ECO:0000269|PubMed:14756555" FT BINDING 226 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:14756555" FT BINDING 256 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:14756555" FT BINDING 282 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:14756555" FT MOD_RES 227 FT /note="N6-(pyridoxal phosphate)lysine" FT MUTAGEN 132 FT /note="D->A: Reduces binding to pyridoxal phosphate and FT strongly reduces catalytic activity." FT /evidence="ECO:0000269|PubMed:14756555" FT MUTAGEN 132 FT /note="D->E: Enhances binding to pyridoxal phosphate." FT /evidence="ECO:0000269|PubMed:14756555" FT MUTAGEN 201 FT /note="D->E: Enhances binding to pyridoxal phosphate." FT /evidence="ECO:0000269|PubMed:14756555" FT HELIX 4..12 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 17..22 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 34..36 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 44..53 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 54..59 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 63..66 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 72..81 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 82..85 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 97..115 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 130..143 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 158..161 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 166..174 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 197..201 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 203..208 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 243..248 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 275..278 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 285..298 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 303..325 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 343..348 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 352..360 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 370..372 FT /evidence="ECO:0007829|PDB:1QZ9" FT STRAND 373..377 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 380..382 FT /evidence="ECO:0007829|PDB:1QZ9" FT HELIX 385..401 FT /evidence="ECO:0007829|PDB:1QZ9" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:1QZ9" SQ SEQUENCE 416 AA; 45905 MW; 50C3DE62A20C779D CRC64; MTTRNDCLAL DAQDSLAPLR QQFALPEGVI YLDGNSLGAR PVAALARAQA VIAEEWGNGL IRSWNSAGWR DLSERLGNRL ATLIGARDGE VVVTDTTSIN LFKVLSAALR VQATRSPERR VIVTETSNFP TDLYIAEGLA DMLQQGYTLR LVDSPEELPQ AIDQDTAVVM LTHVNYKTGY MHDMQALTAL SHECGALAIW DLAHSAGAVP VDLHQAGADY AIGCTYKYLN GGPGSQAFVW VSPQLCDLVP QPLSGWFGHS RQFAMEPRYE PSNGIARYLC GTQPITSLAM VECGLDVFAQ TDMASLRRKS LALTDLFIEL VEQRCAAHEL TLVTPREHAK RGSHVSFEHP EGYAVIQALI DRGVIGDYRE PRIMRFGFTP LYTTFTEVWD AVQILGEILD RKTWAQAQFQ VRHSVT //