KYNU_YEAST
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 03-AUG-2022, entry version 168.
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}; OrderedLocusNames=YLR231C;
GN 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; 58.
DR DIP; DIP-6518N; -.
DR IntAct; Q05979; 7.
DR MINT; Q05979; -.
DR STRING; 4932.YLR231C; -.
DR MaxQB; Q05979; -.
DR PaxDb; Q05979; -.
DR PRIDE; Q05979; -.
DR EnsemblFungi; YLR231C_mRNA; YLR231C; YLR231C.
DR GeneID; 850933; -.
DR KEGG; sce:YLR231C; -.
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; TFPTDGY; -.
DR BioCyc; MetaCyc:YLR231C-MON; -.
DR BioCyc; YEAST:YLR231C-MON; -.
DR Reactome; R-SCE-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
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; 3.40.640.10; -; 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 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
