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Protein

Probable kynurenine--oxoglutarate transaminase BNA3

Gene

BNA3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA).By similarity

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.

Cofactori

Pathwayi: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes kynurenate from L-kynurenine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Aromatic amino acid aminotransferase 2 (ARO9), Probable kynurenine--oxoglutarate transaminase BNA3 (BNA3)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes kynurenate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

GO - Molecular functioni

  • 2-aminoadipate transaminase activity Source: SGD
  • kynurenine-oxoglutarate transaminase activity Source: SGD
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • kynurenic acid biosynthetic process Source: SGD
  • L-kynurenine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8165.
YEAST:YJL060W-MONOMER.
BRENDAi2.6.1.7. 984.
ReactomeiR-SCE-70614. Amino acid synthesis and interconversion (transamination).
R-SCE-71182. Phenylalanine and tyrosine catabolism.
R-SCE-71240. Tryptophan catabolism.
UniPathwayiUPA00334; UER00726.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable kynurenine--oxoglutarate transaminase BNA3 (EC:2.6.1.7)
Alternative name(s):
Biosynthesis of nicotinic acid protein 3
Kynurenine aminotransferase
Gene namesi
Name:BNA3
Ordered Locus Names:YJL060W
ORF Names:J1138
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL060W.
SGDiS000003596. BNA3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Probable kynurenine--oxoglutarate transaminase BNA3PRO_0000123930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiP47039.
PeptideAtlasiP47039.

PTM databases

iPTMnetiP47039.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi33694. 26 interactions.
DIPiDIP-6723N.
IntActiP47039. 8 interactions.
MINTiMINT-658286.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 274Combined sources
Helixi34 – 4512Combined sources
Helixi70 – 7910Combined sources
Helixi83 – 864Combined sources
Helixi95 – 10511Combined sources
Turni106 – 1105Combined sources
Helixi115 – 1173Combined sources
Beta strandi118 – 1225Combined sources
Helixi123 – 13513Combined sources
Beta strandi141 – 1477Combined sources
Helixi152 – 1587Combined sources
Beta strandi162 – 1698Combined sources
Helixi172 – 1754Combined sources
Beta strandi184 – 1863Combined sources
Helixi188 – 1925Combined sources
Beta strandi199 – 2079Combined sources
Turni209 – 2113Combined sources
Helixi217 – 22913Combined sources
Beta strandi233 – 2375Combined sources
Turni239 – 2424Combined sources
Helixi252 – 2543Combined sources
Helixi257 – 2604Combined sources
Beta strandi263 – 2686Combined sources
Helixi269 – 2724Combined sources
Beta strandi281 – 2844Combined sources
Helixi288 – 30114Combined sources
Helixi307 – 32317Combined sources
Helixi325 – 34723Combined sources
Beta strandi355 – 3639Combined sources
Helixi377 – 3793Combined sources
Beta strandi380 – 3823Combined sources
Helixi384 – 39512Combined sources
Helixi403 – 4064Combined sources
Helixi409 – 4157Combined sources
Beta strandi418 – 4225Combined sources
Helixi427 – 43610Combined sources
Helixi437 – 4415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B46X-ray2.00A/B1-444[»]
ProteinModelPortaliP47039.
SMRiP47039. Positions 18-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47039.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00650000093238.
HOGENOMiHOG000223045.
InParanoidiP47039.
KOiK14264.
OMAiSQGANQY.
OrthoDBiEOG7Z0K5V.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47039-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQRFIRQFT NLMSTSRPKV VANKYFTSNT AKDVWSLTNE AAAKAANNSK
60 70 80 90 100
NQGRELINLG QGFFSYSPPQ FAIKEAQKAL DIPMVNQYSP TRGRPSLINS
110 120 130 140 150
LIKLYSPIYN TELKAENVTV TTGANEGILS CLMGLLNAGD EVIVFEPFFD
160 170 180 190 200
QYIPNIELCG GKVVYVPINP PKELDQRNTR GEEWTIDFEQ FEKAITSKTK
210 220 230 240 250
AVIINTPHNP IGKVFTREEL TTLGNICVKH NVVIISDEVY EHLYFTDSFT
260 270 280 290 300
RIATLSPEIG QLTLTVGSAG KSFAATGWRI GWVLSLNAEL LSYAAKAHTR
310 320 330 340 350
ICFASPSPLQ EACANSINDA LKIGYFEKMR QEYINKFKIF TSIFDELGLP
360 370 380 390 400
YTAPEGTYFV LVDFSKVKIP EDYPYPEEIL NKGKDFRISH WLINELGVVA
410 420 430 440
IPPTEFYIKE HEKAAENLLR FAVCKDDAYL ENAVERLKLL KDYL
Length:444
Mass (Da):50,082
Last modified:November 1, 1995 - v1
Checksum:iAAEA86D7AD24F924
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49335 Genomic DNA. Translation: CAA89351.1.
BK006943 Genomic DNA. Translation: DAA08738.1.
PIRiS56832.
RefSeqiNP_012475.3. NM_001181493.3.

Genome annotation databases

EnsemblFungiiYJL060W; YJL060W; YJL060W.
GeneIDi853386.
KEGGisce:YJL060W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49335 Genomic DNA. Translation: CAA89351.1.
BK006943 Genomic DNA. Translation: DAA08738.1.
PIRiS56832.
RefSeqiNP_012475.3. NM_001181493.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B46X-ray2.00A/B1-444[»]
ProteinModelPortaliP47039.
SMRiP47039. Positions 18-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33694. 26 interactions.
DIPiDIP-6723N.
IntActiP47039. 8 interactions.
MINTiMINT-658286.

PTM databases

iPTMnetiP47039.

Proteomic databases

MaxQBiP47039.
PeptideAtlasiP47039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL060W; YJL060W; YJL060W.
GeneIDi853386.
KEGGisce:YJL060W.

Organism-specific databases

EuPathDBiFungiDB:YJL060W.
SGDiS000003596. BNA3.

Phylogenomic databases

GeneTreeiENSGT00650000093238.
HOGENOMiHOG000223045.
InParanoidiP47039.
KOiK14264.
OMAiSQGANQY.
OrthoDBiEOG7Z0K5V.

Enzyme and pathway databases

UniPathwayiUPA00334; UER00726.
BioCyciMetaCyc:MONOMER-8165.
YEAST:YJL060W-MONOMER.
BRENDAi2.6.1.7. 984.
ReactomeiR-SCE-70614. Amino acid synthesis and interconversion (transamination).
R-SCE-71182. Phenylalanine and tyrosine catabolism.
R-SCE-71240. Tryptophan catabolism.

Miscellaneous databases

EvolutionaryTraceiP47039.
PROiP47039.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence."
    Wogulis M., Chew E.R., Donohoue P.D., Wilson D.K.
    Biochemistry 47:1608-1621(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, IDENTIFICATION AS KYNURENINE AMINOTRANSFERASE.

Entry informationi

Entry nameiBNA3_YEAST
AccessioniPrimary (citable) accession number: P47039
Secondary accession number(s): D6VWC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.