ID KYNU_BACCR Reviewed; 428 AA. AC Q81CK0; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 111. 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=BC_2759; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). 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; AE016877; AAP09712.1; -; Genomic_DNA. DR RefSeq; NP_832511.1; NC_004722.1. DR RefSeq; WP_000276298.1; NZ_CP034551.1. DR AlphaFoldDB; Q81CK0; -. DR SMR; Q81CK0; -. DR STRING; 226900.BC_2759; -. DR KEGG; bce:BC2759; -. DR PATRIC; fig|226900.8.peg.2814; -. DR HOGENOM; CLU_003433_4_0_9; -. DR OrthoDB; 9812626at2; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000001417; Chromosome. 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: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; KW Reference proteome. FT CHAIN 1..428 FT /note="Kynureninase" FT /id="PRO_0000356990" FT BINDING 104 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 105 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 132..135 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 213 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 216 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 238 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 267 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT BINDING 295 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" FT MOD_RES 239 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970" SQ SEQUENCE 428 AA; 48754 MW; 39B9A789AE41714F CRC64; MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS WKEYGIDGWT EGEHPWFFLS EKLGKLTAPL IGALPEETIV TGSTTTNIHQ VIATFYEPKG IRTKILADEL TFPSDIYALQ SQIRLKGLDP EEHLVRVKSR DGRTLSEEDI IHAMEDDIAL ILLPSVLYRS GQILDMKRLT TEAHKRGIHI GFDLCHSIGS IPHHFKDWDV DFAVWCNYKY LNAGPGSVAG LYVNSKHFNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS TAPLIGSLEI FKDAGIERLR EKSLHITRYM LNLIGHELKD FEFTIGNPLE DEKRGGHIYL EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE VWKSVQILKK IMKNEEYKQF ENKREVVA //