ID A0A3A8KHB5_9DELT Unreviewed; 425 AA. AC A0A3A8KHB5; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 29-SEP-2021, entry version 10. 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:RKH06936.1}; GN ORFNames=D7X32_03605 {ECO:0000313|EMBL:RKH06936.1}; OS Corallococcus carmarthensis. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Corallococcus. OX NCBI_TaxID=2316728 {ECO:0000313|EMBL:RKH06936.1, ECO:0000313|Proteomes:UP000268313}; RN [1] {ECO:0000313|Proteomes:UP000268313} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CA043D {ECO:0000313|Proteomes:UP000268313}; RA Livingstone P.G., Whitworth D.E.; RL Submitted (SEP-2018) 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. {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; Evidence={ECO:0000256|HAMAP-Rule:MF_01970}; 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RKH06936.1}. 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; RAWE01000007; RKH06936.1; -; Genomic_DNA. DR EnsemblBacteria; RKH06936; RKH06936; D7X32_03605. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000268313; Unassembled WGS sequence. 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; 3.40.640.10; -; 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; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. 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 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 85..388 FT /note="Aminotran_5" FT /evidence="ECO:0000259|Pfam:PF00266" FT REGION 137..140 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 109 FT /note="Pyridoxal phosphate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 110 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 222 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 225 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 247 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 278 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT BINDING 306 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" FT MOD_RES 248 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970" SQ SEQUENCE 425 AA; 47604 MW; 4D7340F42CC887C6 CRC64; MTAPVYENTD VFAYGLDAKD PLRPLRDEFL FPPAASGAPT IYLAGNSLGL QPRKARKYVQ MEMEDWERLG VEGHMHGRHP WLPYHELLTE QVARVVGAQP LEVVVMNTLS VNLHLMMVSF YRPTPERFKI LIEGGAFPSD QYAVASQARF HGYDPKEAIV RLMPREGEDT LRSEDILEAI ERHGKEVALV MLGSVNYLTG QAFDLREITR VAHAQGCKVG FDLAHGAGNL KLSLHDDGPD FAVWCSYKYL NGGPGSLGGV FVHERHARSP ELPRFEGWWG HNKATRFEMG PTFDPLPGAE GWQLSNPPIF QLAALRSSLE LFDKATMAAL RAKSDQLTGF LEFLLDRLPA GYVTITTPRD LKQRGAQLSL RFKGEPKRLL HRLSSAGIIC DFREPDIIRA APAPLYNTYL DVFRFVKALE AHALE //