ID A0A0F0HK53_9ACTN Unreviewed; 399 AA. AC A0A0F0HK53; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}; DE EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}; DE AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970}; GN Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970}; GN ORFNames=UK14_02880 {ECO:0000313|EMBL:KJK54183.1}; OS Streptomyces sp. NRRL F-4428. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK54183.1, ECO:0000313|Proteomes:UP000033569}; RN [1] {ECO:0000313|EMBL:KJK54183.1, ECO:0000313|Proteomes:UP000033569} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK54183.1, RC ECO:0000313|Proteomes:UP000033569}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-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_01970, ECO:0000256|PIRNR:PIRNR038800}. CC -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3- CC hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_01970, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L- CC alanine. {ECO:0000256|HAMAP-Rule:MF_01970, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01970, 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_01970, ECO:0000256|PIRNR:PIRNR038800}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SIMILARITY: Belongs to the kynureninase family. CC {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJK54183.1}. 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; JYJI01000011; KJK54183.1; -; Genomic_DNA. DR EnsemblBacteria; KJK54183; KJK54183; UK14_02880. DR PATRIC; fig|1609137.3.peg.3159; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000033569; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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; -; 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_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:UP000033569}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970, KW ECO:0000256|PIRNR:PIRNR038800}; KW Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970, KW ECO:0000256|PIRNR:PIRNR038800}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970, KW ECO:0000256|PIRNR:PIRNR038800}; KW Reference proteome {ECO:0000313|Proteomes:UP000033569}. FT DOMAIN 79 362 Aminotran_5. {ECO:0000259|Pfam:PF00266}. FT REGION 131 134 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01970}. FT BINDING 102 102 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01970}. FT BINDING 103 103 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 200 200 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 203 203 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 225 225 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 255 255 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 281 281 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_01970}. SQ SEQUENCE 399 AA; 41694 MW; E77E7F3155DD2CD6 CRC64; MPGGAADLRD RAAALDAADE LAKLRERFVL PDGVVYLDGN SLGALPAGVA ATTADVVARQ WGELLIRSWE ESGWWTAPER TGDKIAPLVG AAAGQVVVGD STSVNLFKAL VGAARLAAPG RTRMLVDAAT FPTDGYIAQS AARLTGLTVV PVDPSHAAEA MDADTAVVLL NHVDYRTGRL HDLPALTAAA RAAGAVTVWD LCHSAGALPV GLDAHGVDLA VGCTYKYLNG GPGAPAYLYI ATRHQDAFDS PLPGWNGHAD PFAMTPAYEA APGASRARVG TPDILSMLAL EAALDAWDGV CVEAVRAKSL ALTDFFLECV AAYVPQGLVE PVTPAEHEHR GSQVSLRTGN AREVMGELIS RGVIGDFRAP DVLRFGFTPL YVGFADVERA ARTLGHIFG //