ID   KYNU_FLAJ1              Reviewed;         425 AA.
AC   A5FMM4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_01970};
DE            EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_01970};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000255|HAMAP-Rule:MF_01970};
GN   OrderedLocusNames=Fjoh_0506;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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:0000255|HAMAP-
CC       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:0000255|HAMAP-Rule:MF_01970};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01970};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01970};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine
CC       and anthranilate from L-kynurenine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01970}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01970}.
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DR   EMBL; CP000685; ABQ03541.1; -; Genomic_DNA.
DR   RefSeq; WP_012022597.1; NZ_MUGZ01000026.1.
DR   AlphaFoldDB; A5FMM4; -.
DR   SMR; A5FMM4; -.
DR   STRING; 376686.Fjoh_0506; -.
DR   KEGG; fjo:Fjoh_0506; -.
DR   eggNOG; COG3844; Bacteria.
DR   HOGENOM; CLU_003433_4_0_10; -.
DR   OrthoDB; 9812626at2; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000006694; Chromosome.
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; Pyridine nucleotide biosynthesis; Pyridoxal phosphate.
FT   CHAIN           1..425
FT                   /note="Kynureninase"
FT                   /id="PRO_0000357005"
FT   BINDING         105
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         106
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         133..136
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         218
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         221
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         243
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         274
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         302
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   MOD_RES         244
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
SQ   SEQUENCE   425 AA;  48720 MW;  0070DB3521B3E741 CRC64;
     MTFQNTREFA KQLDAQDALN HYQEQFIFPK VNDKRVIYFT GNSLGLQPKR TKAYIDEVMN
     DWAELAVEGH FYAEKPWWDY QERFSEPLSK IVGALPSEVT VMNTLTVNLH LLMVSFYQPK
     GKRYKIICEE KAFPSDQYMF QSQVHFHGYK PEDAIVEIKR REGEHNIRLE DVLAKIEEVG
     DELALVLIGG VNYYTGQVFD IKTITAAGQK AGAKVGWDLA HAAGNIKLEL HDWNVDFAAW
     CSYKYMNSGP GNASGVFVHE RHHNDPDLPR FAGWWGHNKE RRFKMEPNFD PVHGAGGWQI
     SNLPVLSLAP YLASVEMFAE VGMDALIAKR DHITSYLEFI LHEIDKEVES TFEIITPSNP
     EERASQLSVF LHGEGRSLFD YLMKNGVITD WREPNVIRLA PVPLYCSYED MYDFGQILKK
     GILGK
//