ID KYNU1_CHAGB Reviewed; 509 AA. AC Q2H9P7; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 81. 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 {ECO:0000255|HAMAP-Rule:MF_03017}; ORFNames=CHGG_03057; OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / OS NRRL 1970) (Soil fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium. OX NCBI_TaxID=306901; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970; RX PubMed=25720678; DOI=10.1128/genomea.00021-15; RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.; RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum."; RL Genome Announc. 3:E0002115-E0002115(2015). 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; CH408030; EAQ91122.1; -; Genomic_DNA. DR RefSeq; XP_001229573.1; XM_001229572.1. DR AlphaFoldDB; Q2H9P7; -. DR SMR; Q2H9P7; -. DR STRING; 306901.Q2H9P7; -. DR GeneID; 4389081; -. DR VEuPathDB; FungiDB:CHGG_03057; -. DR eggNOG; KOG3846; Eukaryota. DR HOGENOM; CLU_003433_4_0_1; -. DR InParanoid; Q2H9P7; -. DR OMA; LPGWNSH; -. DR OrthoDB; 5471916at2759; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000001056; Unassembled WGS sequence. 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..509 FT /note="Kynureninase 1" FT /id="PRO_0000356974" FT BINDING 154 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 155 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 183..186 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 270 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 273 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 295 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 345 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 373 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT MOD_RES 296 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" SQ SEQUENCE 509 AA; 55240 MW; B95634E76F9ED0D2 CRC64; MSEILKSPIQ SPLLRGFVTS RRCDASEIED LGSNVTKGLR VAGGRRVLRS HFFSYCLTYP AVNVAATTET GSGDGATEKC VYLCGNSLGL QPKRTQTRVN QYLSTWGTQG VQGHFKPLEE SPLPTWLDAD DRAAQLIAPI VGASKAEVAV MQTLTANLHL LMSAFYKPDI NGKHKIILES KAFPSDHFAV ETQLRHHNLD PATSMITLTS PSSPEDNILT TAEILSAITT HAATTALILL PGIQYYTGQL LDIPTITAHA RTHSVFLIWD LAHAVGNAPL HLHDWGVDAA AWCSYKYLNG GPGCIGGLFV HERNSAVPPP VGELEVQQKE GEWEREGYAN RLAGWWGNDK RTRFAMVNRF RPVPGAAGFQ LSNPSILDIT SLTASLEVFA EAGGVGALRG KSLRLTAFLE ELLVGEGSSI VGVEERALFR VITPSDPGQR GAQLSLMLRG GLLEAVMREL EKRAVIVDER KPDVIRVAPA PLYNSFEDCV RFVVAFGEAL AVARKEVAV //