ID A0A420HWK7_9PEZI Unreviewed; 511 AA. AC A0A420HWK7; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. 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=OnM2_038022 {ECO:0000313|EMBL:RKF61848.1}; OS Oidium neolycopersici. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Erysiphales; Erysiphaceae; Oidium. OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF61848.1, ECO:0000313|Proteomes:UP000286134}; RN [1] {ECO:0000313|EMBL:RKF61848.1, ECO:0000313|Proteomes:UP000286134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF61848.1}; RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z; RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., RA Presley C., Deng X., Wei C.I., Xiao S.; RT "Comparative genome analyses reveal sequence features reflecting RT distinct modes of host-adaptation between dicot and monocot powdery RT mildew."; RL BMC Genomics 19:705-705(2018). 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: CC Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + CC H(+) + 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_03017}; 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; CC EC=3.7.1.3; Evidence={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 -!- 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:RKF61848.1}. 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; MCFK01003833; RKF61848.1; -; Genomic_DNA. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000286134; Unassembled WGS sequence. 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 Complete proteome {ECO:0000313|Proteomes:UP000286134}; 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 DOMAIN 136 302 Aminotran_5. {ECO:0000259|Pfam:PF00266}. FT REGION 183 186 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_03017}. FT BINDING 154 154 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03017}. FT BINDING 155 155 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 268 268 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 271 271 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 293 293 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 331 331 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT BINDING 359 359 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_03017}. FT MOD_RES 294 294 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_03017}. SQ SEQUENCE 511 AA; 57268 MW; D6EE20225189C18E CRC64; MALENTENNT GCEIIPSRTT LKNFTKDYAT YLDELDLLPH SKNLFRIPTK KHLKSNTTIG PLLVSTDEQE DIRDSSSPDS IYLCGNSLGL QPRRTASLIL HYLTTWATQG VHGHFKPLED SPLPEWLDVD IRASNSMAPI LGALPSEVVV MQTLTANLHL LMSAFYRPDF HGRHKIIIES QAFPSDHFVA ESQIKLHGLD PKDSLIIITP QAPSETLTTD QIISTIEEHG PTTSVILFPG IQYYTGQLFD IQAINAAAQK AGIFAIWDLA HAAGNVDLRL HDWNIDAAVW CNYKYLNSGP GVSGGLFIHE NHSNVSEDHG ETKYINRLSG WWGSEKKSRF AMDNRFKPIP GAAGFQLSNP SVLDLTSVIG SLEVFHEACR WQSTDHARQE GITPLRKKSI RLTGYLEAGL HNMEMFKKGM FHIITPSDPN QRGAQLSLKL KPDLLNIVMK ELEERGIVVD ERKPDVIRVA PNPLYNTFED CWNFIDAFQE ALIIAVKAKM ENLLQKKNQE S //