ID G3SPY9_LOXAF Unreviewed; 462 AA. AC G3SPY9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 02-SEP-2026, entry version 80. DE RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}; DE EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}; DE AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017}; GN Name=KYNU {ECO:0000256|HAMAP-Rule:MF_03017, GN ECO:0000313|Ensembl:ENSLAFP00000001817.3}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000001817.3, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000001817.3} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000001817.3}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000001817.3} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000001817.3}; RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. 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. Has a preference for CC the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. CC {ECO:0000256|ARBA:ARBA00054033, ECO:0000256|HAMAP-Rule:MF_03017}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + L- CC alanine + H(+); 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|ARBA:ARBA00050219, CC ECO:0000256|PIRNR:PIRNR038800}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-kynurenine + H2O = anthranilate + L-alanine + H(+); 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|ARBA:ARBA00051308, ECO:0000256|HAMAP- CC Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP- CC Rule:MF_03017, 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_03017, ECO:0000256|PIRNR:PIRNR038800}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017, CC ECO:0000256|PIRNR:PIRNR038800}. CC -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000256|HAMAP- CC Rule:MF_03017, 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 AlphaFoldDB; G3SPY9; -. DR FunCoup; G3SPY9; 225. DR STRING; 9785.ENSLAFP00000001817; -. DR Ensembl; ENSLAFT00000002172.3; ENSLAFP00000001817.3; ENSLAFG00000002172.3. DR eggNOG; KOG3846; Eukaryota. DR GeneTree; ENSGT00390000008033; -. DR HOGENOM; CLU_003433_4_0_1; -. DR InParanoid; G3SPY9; -. DR OMA; LPGWNSH; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0034354; P:'de novo' NAD+ biosynthetic process from L-tryptophan; IEA:UniProtKB-UniRule. DR GO; GO:0006569; P:L-tryptophan catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0034341; P:response to type II interferon; IEA:Ensembl. DR GO; GO:0034516; P:response to vitamin B6; IEA:Ensembl. DR FunFam; 3.40.640.10:FF:000031; Kynureninase; 1. DR FunFam; 3.90.1150.10:FF:000203; Kynureninase; 1. DR FunFam; 3.90.1150.10:FF:000104; Kynureninase, putative; 1. 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; 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; PF22580; KYNU_C; 1. DR PIRSF; PIRSF038800; KYNU; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990, ECO:0000256|HAMAP- KW Rule:MF_03017}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03017}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03017}; KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642, KW ECO:0000256|HAMAP-Rule:MF_03017}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_03017}; Reference proteome {ECO:0000313|Proteomes:UP000007646}. FT BINDING 137 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 138 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 165..168 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 221 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 250 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 253 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 275 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 305 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 333 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT MOD_RES 276 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" SQ SEQUENCE 462 AA; 52137 MW; 5085A0FEF9A0DB29 CRC64; MEPSPLELPA DTIRRIAAEL RCSPTDVQVA LRLDEEDKLR HFREYFYIPK KQDLPPIDLS LVNKDENAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY GHEVGKRPWI TGDESITGLM IDIVGANEKE IVLMNGLTVN LHLLLLSFFK PTPKRYKILL EAKAFPSDHY AIESQLQLHG LNVEKSMRII KPREGEETLR MEDILDVIEK EGDSIAVILF SGVHFYTGQL FNIPAITKAG QAKGCFVGFD LAHAAGNVEL HLHDWGVDFA CWCSYKYLNS GAGGLAGAFV HEKHAHTIKP ALVGWFGHEL NTRFKMDNKL QLIPGATGFR ISNPPILLVC SLHASLEIFK QATMQALRRK SVLLTGYLEY LIKNYHNKDK AESKKPVVNI ITPPHIEERG CQLTLTFSAP MKYVFQELEK RGVVCDKREP NGIRVAPVPL YNSFHDVYKF VSLLISVLDS TE //