ID G0C9K0_XANCA Unreviewed; 424 AA. AC G0C9K0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 24-JAN-2024, entry version 61. 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 ECO:0000313|EMBL:AEL06727.1}; GN ORFNames=XCR_1831 {ECO:0000313|EMBL:AEL06727.1}; OS Xanthomonas campestris pv. raphani 756C. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL06727.1, ECO:0000313|Proteomes:UP000001633}; RN [1] {ECO:0000313|EMBL:AEL06727.1, ECO:0000313|Proteomes:UP000001633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=756C {ECO:0000313|EMBL:AEL06727.1, RC ECO:0000313|Proteomes:UP000001633}; RX PubMed=21784931; DOI=10.1128/JB.05262-11; RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B., RA Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M., RA Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M., RA Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D., RA Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V., RA Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C., RA Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D., RA Leach J.E., White F.F., Salzberg S.L.; RT "Two new complete genome sequences offer insight into host and tissue RT specificity of plant pathogenic Xanthomonas spp."; RL J. Bacteriol. 193:5450-5464(2011). 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; EC=3.7.1.3; CC Evidence={ECO:0000256|PIRNR:PIRNR038800}; 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 --------------------------------------------------------------------------- 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; CP002789; AEL06727.1; -; Genomic_DNA. DR AlphaFoldDB; G0C9K0; -. DR KEGG; xcp:XCR_1831; -. DR PATRIC; fig|990315.4.peg.1722; -. DR HOGENOM; CLU_003433_4_0_6; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000001633; Chromosome. 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR01814; kynureninase; 1. DR PANTHER; PTHR14084; KYNURENINASE; 1. DR PANTHER; PTHR14084:SF0; KYNURENINASE; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF038800; KYNU; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01970}; KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642, KW ECO:0000256|HAMAP-Rule:MF_01970}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01970}. FT DOMAIN 83..360 FT /note="Aminotransferase class V" FT /evidence="ECO:0000259|Pfam:PF00266" FT BINDING 106 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 107 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 134..137 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 219 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 222 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 244 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 274 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 302 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT MOD_RES 245 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" SQ SEQUENCE 424 AA; 46279 MW; F733411962733F70 CRC64; MMTDPLSRSH AAVLDAADPL RALRDAFVFP QHGGQDQTYF VGNSLGLQPR QARAMVYEVL DQWGALAVEG HFTGPTQWLT YHQLVRDGLA RVVGAHPGEV VAMNTLSVNL HLMMASFYRP TSERGAILIE AGAFPSDRHA VESQLRLHGL DPATQLIEVD ADAPDGTLSM AAIADAIARH GRRLALVLWP GIQYRTGQAF DLGEIARLAR AQGAAVGFDL AHAVGNIPLT LHDDGADFAV WCHYKYLNAG PGAVGGCFVH ARHATSDLPR MAGWWGHQQQ TRFRMDPQFV PTPGAEGWQL SNPPVLALAP LRASLDLFDQ AGMAALRAKS EQLTGHLEQL IHARLRQVLQ IVTPAEPARR GCQLSLRVAG GRTQGRALFD HLHAAGVLGD WREPDVIRIA PVPLYNRFSD LHTFVEQVEA WAAR //