ID A0A0F0HK53_9ACTN Unreviewed; 399 AA. AC A0A0F0HK53; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-APR-2021, entry version 24. 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. {ECO:0000256|HAMAP- CC Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}. 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; Evidence={ECO:0000256|HAMAP-Rule:MF_01970}; 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: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-alanine CC and anthranilate from L-kynurenine: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC 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. {ECO:0000256|HAMAP- CC Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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: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; 3.40.640.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01970, KW ECO:0000256|PIRNR:PIRNR038800}; KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642, KW ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}; KW Reference proteome {ECO:0000313|Proteomes:UP000033569}. FT DOMAIN 79..362 FT /note="Aminotran_5" FT /evidence="ECO:0000259|Pfam:PF00266" FT REGION 131..134 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 102 FT /note="Pyridoxal phosphate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 103 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 200 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 203 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 225 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 255 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 281 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT MOD_RES 226 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="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 //