ID A0A0D2F348_9EURO Unreviewed; 489 AA. AC A0A0D2F348; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}; DE EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}; DE AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000256|HAMAP-Rule:MF_03017}; DE AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017}; GN Name=BNA5 {ECO:0000256|HAMAP-Rule:MF_03017}; GN ORFNames=Z517_04055 {ECO:0000313|EMBL:KIW81032.1}; OS Fonsecaea pedrosoi CBS 271.37. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; OC Fonsecaea. OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW81032.1, ECO:0000313|Proteomes:UP000053029}; RN [1] {ECO:0000313|EMBL:KIW81032.1, ECO:0000313|Proteomes:UP000053029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW81032.1, RC ECO:0000313|Proteomes:UP000053029}; RG The Broad Institute Genomics Platform; RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M., RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. 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 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}. CC -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3- CC hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L- CC alanine. {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}; CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L- CC alanine and anthranilate from L-kynurenine: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SIMILARITY: Belongs to the kynureninase family. CC {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-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; KN846971; KIW81032.1; -; Genomic_DNA. DR RefSeq; XP_013284840.1; XM_013429386.1. DR EnsemblFungi; KIW81032; KIW81032; Z517_04055. DR GeneID; 25303545; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000053029; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-HAMAP. DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. 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_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2. DR PANTHER; PTHR14084; PTHR14084; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF038800; KYNU; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01814; kynureninase; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017, KW ECO:0000256|PIRNR:PIRNR038800}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017, KW ECO:0000256|PIRNR:PIRNR038800}; KW Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03017, KW ECO:0000256|PIRNR:PIRNR038800}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03017, KW ECO:0000256|PIRNR:PIRNR038800}; KW Reference proteome {ECO:0000313|Proteomes:UP000053029}. FT DOMAIN 220 285 Aminotran_5. {ECO:0000259|Pfam:PF00266}. FT REGION 171 174 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_03017}. FT BINDING 140 140 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03017}. FT BINDING 141 141 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 257 257 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 260 260 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 282 282 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 320 320 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 348 348 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT MOD_RES 283 283 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_03017}. SQ SEQUENCE 489 AA; 54472 MW; 550EA127B2173B1D CRC64; MSKADIPRDF YSMKEPGDPF SPDFALSLDA RDPLSHFRSE FHIPTRADLN RPTLSKSPGE GPSQPCTYLC GNSLGLQPVR TANLVNSFLT QWRTKGVLGH FVEHSDSPLA PFLHIDDHAA RLMAPIVGAL ESEVAVMGSL TANLHLLMSS FYRPSKKGEG RWKILLEGKA FPSDHYAVES QIIHHGLDPA EAMVLLEPVY DRFPTLSTDQ ILRAIDEHSS ELALILLPGI QFYTGQYFDI PRITAHAHSH GIMIGWDLAH AAGNVDLKLH DWNVDFAAWC SYKYLNSGPG AMAGIFINEK FGKVDMKSPT HKYWPRLTGW WGDDKSSRFQ MTNKFVPRPG AAGYQVSNPS ALDLAAVVAS LQIFNETSMK DLREKSVRLT NYLEHLLDDI AMRKPGKFDI ITVRDAKDRG AQLSIRLAPG LLDGVLRHLE REGVIVDERK PDVIRVAPAP LYNTFTDVFH FCQVLDDALG KDRLSTKRLA PVSEQLAGL //