ID A0A3A8KHB5_9DELT Unreviewed; 425 AA. AC A0A3A8KHB5; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 16-JAN-2019, entry version 2. 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 sp. CA043D. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Corallococcus. OX NCBI_TaxID=2316728 {ECO:0000313|EMBL:RKH06936.1}; RN [1] {ECO:0000313|EMBL:RKH06936.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CA043D {ECO:0000313|EMBL:RKH06936.1}; RA Parvin R., Begum J.A., Chowdhury E.H., Islam M.R., Harder T.; 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. CC {ECO:0000256|HAMAP-Rule:MF_01970, 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_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; CC EC=3.7.1.3; 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- CC alanine and anthranilate from L-kynurenine: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from 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. CC {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}. 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: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 UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. 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 Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970, KW ECO:0000256|PIRNR:PIRNR038800, ECO:0000313|EMBL:RKH06936.1}; KW Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970, KW ECO:0000256|PIRNR:PIRNR038800}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970, KW ECO:0000256|PIRNR:PIRNR038800}. FT DOMAIN 85 388 Aminotran_5. {ECO:0000259|Pfam:PF00266}. FT REGION 137 140 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01970}. FT BINDING 109 109 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01970}. FT BINDING 110 110 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 222 222 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 225 225 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 247 247 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 278 278 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT BINDING 306 306 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01970}. FT MOD_RES 248 248 N6-(pyridoxal phosphate)lysine. FT {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 //