ID KYNU_XANAC Reviewed; 423 AA. AC Q8PM33; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 03-OCT-2012, entry version 59. DE RecName: Full=Kynureninase; DE EC=3.7.1.3; DE AltName: Full=L-kynurenine hydrolase; GN Name=kynU; OrderedLocusNames=XAC1601; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L- CC alanine. CC -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3- CC hydroxyanthranilate + L-alanine. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L- CC alanine and anthranilate from L-kynurenine: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from L-kynurenine: step 2/3. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the kynureninase family. 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; AE008923; AAM36469.1; -; Genomic_DNA. DR RefSeq; NP_641933.1; NC_003919.1. DR ProteinModelPortal; Q8PM33; -. DR GeneID; 1155672; -. DR GenomeReviews; AE008923_GR; XAC1601. DR KEGG; xac:XAC1601; -. DR PATRIC; 24055203; VBIXanAxo33670_1680. DR eggNOG; COG3844; -. DR HOGENOM; HOG000242438; -. DR KO; K01556; -. DR OMA; TAEAHKR; -. DR ProtClustDB; CLSK903751; -. DR BioCyc; XAXO190486:XAC1601-MONOMER; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0030429; F:kynureninase activity; IEA:EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR GO; GO:0006569; P:tryptophan catabolic process; IEA:InterPro. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 2. DR HAMAP; MF_01970; Kynureninase; 1; -. DR InterPro; IPR000192; Aminotrans_V/Cys_dSase. DR InterPro; IPR010111; Kynureninase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR14084; PTHR14084; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF038800; KYNU; 1. DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1. DR TIGRFAMs; TIGR01814; kynureninase; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Pyridine nucleotide biosynthesis; KW Pyridoxal phosphate. FT CHAIN 1 423 Kynureninase. FT /FTId=PRO_0000357014. FT REGION 133 136 Pyridoxal phosphate binding (By FT similarity). FT BINDING 105 105 Pyridoxal phosphate; via amide nitrogen FT (By similarity). FT BINDING 106 106 Pyridoxal phosphate (By similarity). FT BINDING 218 218 Pyridoxal phosphate (By similarity). FT BINDING 221 221 Pyridoxal phosphate (By similarity). FT BINDING 243 243 Pyridoxal phosphate (By similarity). FT BINDING 273 273 Pyridoxal phosphate (By similarity). FT BINDING 301 301 Pyridoxal phosphate (By similarity). FT MOD_RES 244 244 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 423 AA; 45845 MW; D05719233F2F29BC CRC64; MTDPLSRAHA AALDAADPLR NLRDAFVFPQ HGDDDQTYFV GNSLGLQPRA ARAMVDEVLD QWGALAVEGH FTGPTQWLTY HQLVGDALAR VVGAQPGEVV AMNTLSVNLH LMMASFYRPT AERGAILIEA GAFPSDRHAV ESQLRLHGLD PATHLIEVEA DEPNGTVSMS AIAEAIAQHG PHLALVLWPG IQYRTGQAFD LAEIVRLARA QGAAVGLDLA HAVGNLPLTL HDDGVDFAVW CHYKYLNAGP GAVGGCFVHA RHATSDLPRM AGWWGHEQQT RFRMDPQFVP SPGAEGWQLS NPPVLALAPL RASLALFDQA GMAALRAKSE QLTGHLEQMI HARVPQVLQI VTPVEPARRG CQLSLRVAGG RARGRALFEH LHAAGVLGDW REPDVIRIAP VPLYNRFSDL HTFVEQVEAW AAA //