Probable kynurenine--oxoglutarate transaminase BNA3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P47039 (BNA3_YEAST)

Last modified January 19, 2010. Version 93. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Probable kynurenine--oxoglutarate transaminase BNA3
    EC=2.6.1.7
Alternative name(s):
    Kynurenine aminotransferase
    Biosynthesis of nicotinic acid protein 3

Gene names

Name:	BNA3
Ordered Locus Names:	YJL060W
ORF Names:	J1138

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) By similarity.
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
Cofactor	Pyridoxal phosphate Potential.
Pathway	Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.
Subunit structure	Homodimer. Ref.5
Subcellular location	Cytoplasm. Mitochondrion Ref.2.
Miscellaneous	Present with 1600 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

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Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	kynurenic acid biosynthetic process Ref.5 Inferred from direct assay. Source: SGD
Cellular component	mitochondrion Ref.2 Inferred from direct assay. Source: SGD
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro kynurenine-oxoglutarate transaminase activity Ref.5 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
INO1	P11986	1	EBI-25893,EBI-9257
LSP1	Q12230	1	EBI-25893,EBI-34978
SNC2	P33328	1	EBI-25893,EBI-17512
TRP2	P00899	1	EBI-25893,EBI-19575

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 444

444

Probable kynurenine--oxoglutarate transaminase BNA3

PRO_0000123930

Amino acid modifications

Modified residue

Phosphoserine Ref.4

Modified residue

271

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

444

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P47039-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: AAEA86D7AD24F924
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FASTA

444

50,082

        10         20         30         40         50         60 
MKQRFIRQFT NLMSTSRPKV VANKYFTSNT AKDVWSLTNE AAAKAANNSK NQGRELINLG 

        70         80         90        100        110        120 
QGFFSYSPPQ FAIKEAQKAL DIPMVNQYSP TRGRPSLINS LIKLYSPIYN TELKAENVTV 

       130        140        150        160        170        180 
TTGANEGILS CLMGLLNAGD EVIVFEPFFD QYIPNIELCG GKVVYVPINP PKELDQRNTR 

       190        200        210        220        230        240 
GEEWTIDFEQ FEKAITSKTK AVIINTPHNP IGKVFTREEL TTLGNICVKH NVVIISDEVY 

       250        260        270        280        290        300 
EHLYFTDSFT RIATLSPEIG QLTLTVGSAG KSFAATGWRI GWVLSLNAEL LSYAAKAHTR 

       310        320        330        340        350        360 
ICFASPSPLQ EACANSINDA LKIGYFEKMR QEYINKFKIF TSIFDELGLP YTAPEGTYFV 

       370        380        390        400        410        420 
LVDFSKVKIP EDYPYPEEIL NKGKDFRISH WLINELGVVA IPPTEFYIKE HEKAAENLLR 

       430        440 
FAVCKDDAYL ENAVERLKLL KDYL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, MASS SPECTROMETRY.
[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: 18205391] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, IDENTIFICATION AS KYNURENINE AMINOTRANSFERASE.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z49335 Genomic DNA. Translation: CAA89351.1.

PIR

S56832.

RefSeq

NP_012475.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3B46	X-ray	2.00	A/B	1-444	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6723N.

IntAct

P47039. 13 interactions.

STRING

P47039.

Proteomic databases

PeptideAtlas

P47039.

Genome annotation databases

Ensembl

YJL060W; YJL060W; YJL060W; Saccharomyces cerevisiae. [Genome view]

GeneID

853386.

KEGG

sce:YJL060W.

NMPDR

fig|4932.3.peg.3447.

Organism-specific databases

CYGD

YJL060w.

SGD

S000003596. BNA3.

Phylogenomic databases

eggNOG

HOGENOM

OMA

OrthoDB

PhylomeDB

P47039.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-8165.

Gene expression databases

ArrayExpress

P47039.

Genevestigator

P47039.

GermOnline

YJL060W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00753. ACCSYNTHASE.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

973849.

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Entry information

Entry name

BNA3_YEAST

Accession

Primary (citable) accession number: P47039

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 19, 2010
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents