ID A0A0D2F348_9EURO Unreviewed; 489 AA. AC A0A0D2F348; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 24-JUN-2015, entry version 3. 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}; RN [1] {ECO:0000313|EMBL:KIW81032.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW81032.1}; 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 --------------------------------------------------------------------------- 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 UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. 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: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; -; 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_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_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 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}. 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 //