ID KYNU_PICGU Reviewed; 445 AA. AC A5DM91; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 04-NOV-2026, entry version 88. DE RecName: Full=Kynureninase {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 {ECO:0000255|HAMAP-Rule:MF_03017}; DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_03017}; GN Name=BNA5 {ECO:0000255|HAMAP-Rule:MF_03017}; ORFNames=PGUG_04392; OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes; OC Debaryomycetaceae; Meyerozyma. OX NCBI_TaxID=294746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL RC Y-324; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B., RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., RA Birren B.W., Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). 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=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_03017}; 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_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; CH408159; EDK40294.2; -; Genomic_DNA. DR RefSeq; XP_001483663.2; XM_001483613.1. DR AlphaFoldDB; A5DM91; -. DR SMR; A5DM91; -. DR FunCoup; A5DM91; 209. DR STRING; 294746.A5DM91; -. DR GeneID; 5125646; -. DR KEGG; pgu:PGUG_04392; -. DR VEuPathDB; FungiDB:PGUG_04392; -. DR eggNOG; KOG3846; Eukaryota. DR HOGENOM; CLU_003433_4_0_1; -. DR InParanoid; A5DM91; -. DR OMA; AAAWCSY; -. DR OrthoDB; 5978656at2759; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000001997; Unassembled WGS sequence. DR GO; GO:0097268; C:cytoophidium; IEA:EnsemblFungi. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 L-tryptophan; IEA:UniProtKB-UniRule. DR GO; GO:0006569; P:L-tryptophan catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.640.10:FF:000031; 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 Cytoplasm; Hydrolase; Pyridine nucleotide biosynthesis; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1..445 FT /note="Kynureninase" FT /id="PRO_0000360871" FT BINDING 104 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 105 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 132..135 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 216 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 219 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 241 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 276 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT BINDING 304 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" FT MOD_RES 242 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017" SQ SEQUENCE 445 AA; 50662 MW; C0B61477246C40C5 CRC64; MSAQLDKEYP TFRHLFEVPT LKSLNISSDT NESIYLCGNS LGLMPKSTRK AINDELDTWA QQGVEGHFSH PERTPWVDID LPLLPLMAPI VGAKESEVAV MGSLTSNLNA MLMSFYKPKG KRTKILFEKH AFPSDYYAFL NIVQLFGYDE SHLIQVAVQD GATYLRTEDI IFEIENNAEE LALVCFPGIQ YYTGQFFDIK SITKAAQDHG ICVGWDLAHA VGNVPLNLHD WNVDFAVWCS YKYLNSGPGA MAGIFVHQRH TENNSKTSYN PRLAGWWGNN AQERFQMKEE FNPINSALSY RQSNPSVIDT VAVKASLKVF QEANGIQFLR EKSIKMTQFL QDLLTQSQYY INQNEKPTKL GFQILTPLDP NQRGCQLSLL FHPHYDEKSK NIMEQVNKYL HNRGIVCDER RPDVIRVAPT PLYNTFAEIE YAVKSLNEAL NQIEN //