ID   KYNU_YEAST              Reviewed;         453 AA.
AC   Q05979; D6VYN2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_03017};
DE            EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_03017};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000255|HAMAP-Rule:MF_03017};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_03017};
GN   Name=BNA5 {ECO:0000255|HAMAP-Rule:MF_03017};
GN   OrderedLocusNames=YLR231C; ORFNames=L8083.14;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=12062417; DOI=10.1016/s0014-5793(02)02585-1;
RA   Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M.,
RA   Rytka J., Herbert C.J.;
RT   "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.";
RL   FEBS Lett. 517:97-102(2002).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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_03017, ECO:0000269|PubMed:12062417}.
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_03017};
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_03017};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03017};
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_03017, ECO:0000269|PubMed:12062417}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_03017,
CC       ECO:0000269|PubMed:12062417}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03017}.
CC   -!- INTERACTION:
CC       Q05979; P39940: RSP5; NbExp=2; IntAct=EBI-10016, EBI-16219;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03017,
CC       ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03017}.
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DR   EMBL; U19027; AAB67417.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09548.1; -; Genomic_DNA.
DR   PIR; S51453; S51453.
DR   RefSeq; NP_013332.1; NM_001182118.1.
DR   AlphaFoldDB; Q05979; -.
DR   SMR; Q05979; -.
DR   BioGRID; 31501; 62.
DR   DIP; DIP-6518N; -.
DR   IntAct; Q05979; 7.
DR   MINT; Q05979; -.
DR   STRING; 4932.YLR231C; -.
DR   MaxQB; Q05979; -.
DR   PaxDb; 4932-YLR231C; -.
DR   PeptideAtlas; Q05979; -.
DR   EnsemblFungi; YLR231C_mRNA; YLR231C; YLR231C.
DR   GeneID; 850933; -.
DR   KEGG; sce:YLR231C; -.
DR   AGR; SGD:S000004221; -.
DR   SGD; S000004221; BNA5.
DR   VEuPathDB; FungiDB:YLR231C; -.
DR   eggNOG; KOG3846; Eukaryota.
DR   GeneTree; ENSGT00390000008033; -.
DR   HOGENOM; CLU_003433_4_0_1; -.
DR   InParanoid; Q05979; -.
DR   OMA; LPGWNSH; -.
DR   OrthoDB; 5471916at2759; -.
DR   BioCyc; MetaCyc:YLR231C-MONOMER; -.
DR   BioCyc; YEAST:YLR231C-MONOMER; -.
DR   Reactome; R-SCE-71240; Tryptophan catabolism.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   BioGRID-ORCS; 850933; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q05979; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05979; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA.
DR   GO; GO:0030429; F:kynureninase activity; IMP:SGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IGI:SGD.
DR   GO; GO:0043420; P:anthranilate metabolic process; IBA:GO_Central.
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:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Nucleus; Pyridine nucleotide biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..453
FT                   /note="Kynureninase"
FT                   /id="PRO_0000218665"
FT   BINDING         111
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         112
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         139..142
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         196
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         226
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         229
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         251
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         286
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         314
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
SQ   SEQUENCE   453 AA;  51032 MW;  95C84CBB4F6FCF9B CRC64;
     MEKALELDGE YPESLRDEFN IPTFKSMGLS SDDKPVTYLC GNSLGLMPKS TRNSINAELD
     AWSDCAVESH FKHPEEARGK VPWVSIDLPI LPLLAPIVGA QENEVAVMNS LTANLNSLLI
     TFYKPTEKRF KILFEKGSFP SDYYAFYNQC KIHGISEPEN VFIQIEPREG ETYIRTQDIL
     DTIEVNQDEL ALVCLSGVQY YTGQYFDIGR ITSFAHQFPD ILVGWDLAHA VGNVPLQLHD
     WGVDFACWCS YKYLNAGPGG IGGLFVHSKH TKPDPAKESL PRLAGWWGND PAKRFQMLEV
     FEPIPGALGF RQSNPSVIDT VALRSSLELF AKFNGINEVR KRSLLLTNYM TELLEASKYY
     KHPLRIEKLP CFFTILTPTS TDEEHGAQLS LYFDSDTGKE DIMPKVFQYL HDHGVIGDAR
     RPNVIRLAPA PLYNTFSDVY IAVNALNEAM DKL
//