ID A0A1W1Y8A0_9FLAO Unreviewed; 424 AA. AC A0A1W1Y8A0; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 05-JUL-2017, entry version 2. 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=SAMN05660703_0098 {ECO:0000313|EMBL:SMC32051.1}; OS Cellulophaga tyrosinoxydans. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=504486 {ECO:0000313|EMBL:SMC32051.1, ECO:0000313|Proteomes:UP000192360}; RN [1] {ECO:0000313|EMBL:SMC32051.1, ECO:0000313|Proteomes:UP000192360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21164 {ECO:0000313|EMBL:SMC32051.1, RC ECO:0000313|Proteomes:UP000192360}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (APR-2017) 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 --------------------------------------------------------------------------- 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; FWXO01000001; SMC32051.1; -; Genomic_DNA. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000192360; Unassembled WGS sequence. 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; 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:UP000192360}; 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}. FT DOMAIN 176 345 Aminotran_5. {ECO:0000259|Pfam:PF00266}. FT REGION 133 136 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01970}. FT BINDING 105 105 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01970}. FT BINDING 106 106 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 218 218 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 221 221 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 243 243 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 274 274 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 302 302 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT MOD_RES 244 244 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_01970}. SQ SEQUENCE 424 AA; 48550 MW; 37AF5B977221BBE0 CRC64; MQFENTLQFA QKLDAADKLK KYRDEFHFPK VNGKQVIYFT GNSLGLQPKR TQKFVDDVMA DWANLAVEGH FYAEKPWWDY HERLAAPLAK VVGAKTEEVS VMNTLSVNLH LLLVSFYRPT KTRFKILCEE KAFPSDQYML KSQVRFHGLD PEETIVEVKK RAGEHHWRTE DILAKIKEIG SELALVLIGG VNYYNGQVFD MKTITAAGQK AGAFVGWDLA HGVGNIALNL NEWNVDFAAW CSYKYMNSGP GHASGIYVNE KYLNDPDIPR FEGWWGTKKE TRFLMKPEFE PMETADAWQI SNAPILSVAP YLASLELFEK VGMDALIEKR DKIVAYLEFI LHEIDAEVDS TFEIITPKDR GCQLSVFLHG QGRSLFDFLM KNGVITDWRE PNVIRLAPAP FYCSYEDMYQ FGQLLKKGIL ENLN //