ID D3P4C7_AZOS1 Unreviewed; 397 AA. AC D3P4C7; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 24-JAN-2024, entry version 78. 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 OrderedLocusNames=AZL_c02130 {ECO:0000313|EMBL:BAI75506.1}; OS Azospirillum sp. (strain B510). OG Plasmid pAB510c {ECO:0000313|EMBL:BAI75506.1, OG ECO:0000313|Proteomes:UP000002040}. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Azospirillaceae; Azospirillum. OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75506.1, ECO:0000313|Proteomes:UP000002040}; RN [1] {ECO:0000313|EMBL:BAI75506.1, ECO:0000313|Proteomes:UP000002040} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B510 {ECO:0000313|EMBL:BAI75506.1, RC ECO:0000313|Proteomes:UP000002040}; RC PLASMID=pAB510c {ECO:0000313|EMBL:BAI75506.1}; RX PubMed=20047946; DOI=10.1093/dnares/dsp026; RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H., RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y., RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N., RA Nakayama S., Yamada M., Tabata S., Sato S.; RT "Complete genomic structure of the cultivated rice endophyte Azospirillum RT sp. B510."; RL DNA Res. 17:37-50(2010). 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 --------------------------------------------------------------------------- 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; AP010949; BAI75506.1; -; Genomic_DNA. DR RefSeq; WP_012977337.1; NC_013857.1. DR AlphaFoldDB; D3P4C7; -. DR KEGG; azl:AZL_c02130; -. DR HOGENOM; CLU_003433_4_1_5; -. DR OrthoDB; 9812626at2; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000002040; Plasmid pAB510c. 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 Plasmid {ECO:0000313|EMBL:BAI75506.1}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000002040}. FT DOMAIN 135..332 FT /note="Aminotransferase class V" FT /evidence="ECO:0000259|Pfam:PF00266" FT BINDING 85 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 86 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 113..116 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 155 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 184 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 187 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 209 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 239 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 265 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT MOD_RES 210 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" SQ SEQUENCE 397 AA; 42670 MW; 7B9F4C078D5B12DF CRC64; MTDFAKTRAR FDIPDGVIYL DGNSLGPLPI AAKERVARTL AEEWGGQLIR GWNSAGWMVQ PRKVGDRIAR LIGAPAGSVV VGDTLSIKVY QALAAALAMR PERRVILSDS GNFPTDLYMA EGLIETLGQG HILKVVAPEE VEGTIGEDVA VLMLTEVDYR TGRLHDMAAL TAKAHAAGVV TVWDLAHSAG ALPVDLAGAG TDFAVGCTYK YLNGGPGAPA FIYVAPQHAE RARPALSGWM GHEAPFAFDP SYRPGAGVER MRVGTPPVIA LAALDAALDV WDDVDMADIR RTSMTLCDLF IELVEAQCPT LELASPRDGS RRGSQVSFRH PQGYAIMQAL IDRGVIGDFR APDVLRFGFT PLYIGEAEVR GAVAVLKQVT DGGLWDRPEY HRKAIVT //