ID   BNA3_YEAST              Reviewed;         444 AA.
AC   P47039; D6VWC2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 203.
DE   RecName: Full=Probable kynurenine--oxoglutarate transaminase BNA3;
DE            EC=2.6.1.7;
DE   AltName: Full=Biosynthesis of nicotinic acid protein 3;
DE   AltName: Full=Kynurenine aminotransferase;
GN   Name=BNA3; OrderedLocusNames=YJL060W; ORFNames=J1138;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   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   [4]
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).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY, SUBUNIT, AND IDENTIFICATION AS KYNURENINE
RP   AMINOTRANSFERASE.
RX   PubMed=18205391; DOI=10.1021/bi701172v;
RA   Wogulis M., Chew E.R., Donohoue P.D., Wilson D.K.;
RT   "Identification of formyl kynurenine formamidase and kynurenine
RT   aminotransferase from Saccharomyces cerevisiae using crystallographic,
RT   bioinformatic and biochemical evidence.";
RL   Biochemistry 47:1608-1621(2008).
CC   -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC       metabolite L-kynurenine to form kynurenic acid (KA). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate +
CC         H2O; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC       from L-kynurenine: step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18205391}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:16823961}.
CC   -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; Z49335; CAA89351.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08738.1; -; Genomic_DNA.
DR   PIR; S56832; S56832.
DR   RefSeq; NP_012475.3; NM_001181493.3.
DR   PDB; 3B46; X-ray; 2.00 A; A/B=1-444.
DR   AlphaFoldDB; P47039; -.
DR   SMR; P47039; -.
DR   BioGRID; 33694; 101.
DR   DIP; DIP-6723N; -.
DR   FunCoup; P47039; 527.
DR   IntAct; P47039; 8.
DR   STRING; 4932.YJL060W; -.
DR   iPTMnet; P47039; -.
DR   PaxDb; 4932-YJL060W; -.
DR   PeptideAtlas; P47039; -.
DR   EnsemblFungi; YJL060W_mRNA; YJL060W; YJL060W.
DR   GeneID; 853386; -.
DR   KEGG; sce:YJL060W; -.
DR   AGR; SGD:S000003596; -.
DR   SGD; S000003596; BNA3.
DR   VEuPathDB; FungiDB:YJL060W; -.
DR   eggNOG; KOG0257; Eukaryota.
DR   HOGENOM; CLU_017584_4_0_1; -.
DR   InParanoid; P47039; -.
DR   OMA; AACIFQQ; -.
DR   OrthoDB; 2414662at2759; -.
DR   BioCyc; MetaCyc:YJL060W-MONOMER; -.
DR   BioCyc; YEAST:YJL060W-MONOMER; -.
DR   BRENDA; 2.6.1.7; 984.
DR   Reactome; R-SCE-71240; Tryptophan catabolism.
DR   Reactome; R-SCE-8964208; Phenylalanine metabolism.
DR   Reactome; R-SCE-8964539; Glutamate and glutamine metabolism.
DR   UniPathway; UPA00334; UER00726.
DR   BioGRID-ORCS; 853386; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P47039; -.
DR   PRO; PR:P47039; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47039; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0047536; F:L-2-aminoadipate:2-oxoglutarate transaminase activity; IDA:SGD.
DR   GO; GO:0016212; F:L-kynurenine:2-oxoglutarate transaminase activity; IDA:SGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034276; P:kynurenic acid biosynthetic process; IDA:SGD.
DR   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000024; Kynurenine--oxoglutarate transaminase 3; 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   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR051326; Kynurenine-oxoglutarate_AT.
DR   InterPro; IPR004838; NHTrfase_class1_PLP_cs.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43807; FI04487P; 1.
DR   PANTHER; PTHR43807:SF20; FI04487P; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminotransferase; Cytoplasm; Mitochondrion;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..444
FT                   /note="Probable kynurenine--oxoglutarate transaminase BNA3"
FT                   /id="PRO_0000123930"
FT   MOD_RES         271
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           24..27
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           34..45
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           70..79
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           83..86
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           95..105
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   TURN            106..110
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           123..135
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          141..147
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           152..158
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          162..169
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           188..192
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          199..207
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   TURN            209..211
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           217..229
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          233..237
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   TURN            239..242
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           257..260
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          281..284
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           288..301
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           307..323
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           325..347
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          355..363
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           377..379
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          380..382
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           384..395
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           403..406
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           409..415
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   STRAND          418..422
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           427..436
FT                   /evidence="ECO:0007829|PDB:3B46"
FT   HELIX           437..441
FT                   /evidence="ECO:0007829|PDB:3B46"
SQ   SEQUENCE   444 AA;  50082 MW;  AAEA86D7AD24F924 CRC64;
     MKQRFIRQFT NLMSTSRPKV VANKYFTSNT AKDVWSLTNE AAAKAANNSK NQGRELINLG
     QGFFSYSPPQ FAIKEAQKAL DIPMVNQYSP TRGRPSLINS LIKLYSPIYN TELKAENVTV
     TTGANEGILS CLMGLLNAGD EVIVFEPFFD QYIPNIELCG GKVVYVPINP PKELDQRNTR
     GEEWTIDFEQ FEKAITSKTK AVIINTPHNP IGKVFTREEL TTLGNICVKH NVVIISDEVY
     EHLYFTDSFT RIATLSPEIG QLTLTVGSAG KSFAATGWRI GWVLSLNAEL LSYAAKAHTR
     ICFASPSPLQ EACANSINDA LKIGYFEKMR QEYINKFKIF TSIFDELGLP YTAPEGTYFV
     LVDFSKVKIP EDYPYPEEIL NKGKDFRISH WLINELGVVA IPPTEFYIKE HEKAAENLLR
     FAVCKDDAYL ENAVERLKLL KDYL
//