ID KYNU1_ASPOR Reviewed; 487 AA. AC Q2U038; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 13-SEP-2023, entry version 92. DE RecName: Full=Kynureninase 1 {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 5-1 {ECO:0000255|HAMAP-Rule:MF_03017}; DE AltName: Full=L-kynurenine hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03017}; GN Name=bna5-1; ORFNames=AO090011000602; OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=510516; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42149 / RIB 40; RX PubMed=16372010; DOI=10.1038/nature04300; RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E., RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., RA Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(2005). 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; AP007171; BAE65077.1; -; Genomic_DNA. DR RefSeq; XP_001826210.1; XM_001826158.2. DR AlphaFoldDB; Q2U038; -. DR SMR; Q2U038; -. DR STRING; 510516.Q2U038; -. DR EnsemblFungi; BAE65077; BAE65077; AO090011000602. DR GeneID; 5998313; -. DR KEGG; aor:AO090011000602; -. DR VEuPathDB; FungiDB:AO090011000602; -. DR HOGENOM; CLU_003433_4_0_1; -. DR OMA; TFPTDGY; -. DR OrthoDB; 5471916at2759; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000006564; Chromosome 7. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 Cytoplasm; Hydrolase; Pyridine nucleotide biosynthesis; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1..487 FT /note="Kynureninase 1" FT /id="PRO_0000356969" FT BINDING 147 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 148 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 175..178 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 232 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 261 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 264 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 286 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 327 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 355 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT MOD_RES 287 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" SQ SEQUENCE 487 AA; 54916 MW; 8492F301C147F4F7 CRC64; MGSRLHVQEI KKGPPLPFKD DIRAFTREYA ESLDAQDPLR HFRDEFIIPS KKDLKRKTLN ANENIEDSSD PRSIYLCGNS LGLQPRNTRK YLEHYLRTWA IKGVTGHFTP HDDQLLPPFV DVDDAGAKLM APIVGALESE VAVMGTLTAN LHFLMASFYQ PTKEKYKIIL EGKAFPSDHY AVESQIQHHN LDPKDAMVLI ELENLDRPIL DTEKILRVID EHASSTALIL LSGIQFYTGQ YFDIEKITAY AHSKGIIIGW DCAHAAGNVE LKLHDWNVDF AAWCNYKYLN SGPGGMAGLF VHENHGRVDM TKVGSKDEPF RPRLSGWWGD DKKTRFRMEN RFVPQPGAAG FQLSNPSVLD MNAVAASLEI FNRTSMAEIR KKSLDLTGYL EHLLLKYPLD AAPEDKPFSI ITPSNPAERG AQLSLRLGPG LLDNVLEVLE ENGVVIDERK PDVIRVAPAP LYNTYADVWQ FCQIFFDACQ KAVRARK //