BNA3_YEAST
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 03-AUG-2022, entry version 188.
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 (2.0 ANGSTROMS), SUBUNIT, AND IDENTIFICATION AS
RP KYNURENINE 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=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC 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}.
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 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 PDBsum; 3B46; -.
DR AlphaFoldDB; P47039; -.
DR SMR; P47039; -.
DR BioGRID; 33694; 94.
DR DIP; DIP-6723N; -.
DR IntAct; P47039; 8.
DR MINT; P47039; -.
DR STRING; 4932.YJL060W; -.
DR iPTMnet; P47039; -.
DR MaxQB; P47039; -.
DR PaxDb; P47039; -.
DR PRIDE; P47039; -.
DR EnsemblFungi; YJL060W_mRNA; YJL060W; YJL060W.
DR GeneID; 853386; -.
DR KEGG; sce:YJL060W; -.
DR SGD; S000003596; BNA3.
DR VEuPathDB; FungiDB:YJL060W; -.
DR eggNOG; KOG0257; Eukaryota.
DR GeneTree; ENSGT00940000171422; -.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; P47039; -.
DR OMA; SVAMTGW; -.
DR BioCyc; MetaCyc:YJL060W-MON; -.
DR BioCyc; YEAST:YJL060W-MON; -.
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 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:2-aminoadipate transaminase activity; IDA:SGD.
DR GO; GO:0016212; F:kynurenine-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 GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 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 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
