P47039 (BNA3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable kynurenine--oxoglutarate transaminase BNA3
EC=2.6.1.7

Alternative name(s):
Biosynthesis of nicotinic acid protein 3
Kynurenine aminotransferase

Gene names

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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

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

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.6
Subcellular location	Cytoplasm. Mitochondrion Ref.3.
Miscellaneous	Present with 1600 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	kynurenic acid biosynthetic process Inferred from direct assay Ref.6. Source: SGD
Cellular component	mitochondrion Inferred from direct assay Ref.3. Source: SGD
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro kynurenine-oxoglutarate transaminase activity Inferred from direct assay Ref.6. Source: SGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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

96

1

Phosphoserine Ref.5

Modified residue

271

1

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

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444

Helix Strand Turn

Details...

Helix

24 – 27

4

Helix

34 – 45

12

Helix

70 – 79

10

Helix

83 – 86

4

Helix

95 – 105

11

Turn

106 – 110

5

Helix

115 – 117

3

Beta strand

118 – 122

5

Helix

123 – 135

13

Beta strand

141 – 147

7

Helix

152 – 158

7

Beta strand

162 – 169

8

Helix

172 – 175

4

Beta strand

184 – 186

3

Helix

188 – 192

5

Beta strand

199 – 207

9

Turn

209 – 211

3

Helix

217 – 229

13

Beta strand

233 – 237

5

Turn

239 – 242

4

Helix

252 – 254

3

Helix

257 – 260

4

Beta strand

263 – 268

6

Helix

269 – 272

4

Beta strand

281 – 284

4

Helix

288 – 301

14

Helix

307 – 323

17

Helix

325 – 347

23

Beta strand

355 – 363

9

Helix

377 – 379

3

Beta strand

380 – 382

3

Helix

384 – 395

12

Helix

403 – 406

4

Helix

409 – 415

7

Beta strand

418 – 422

5

Helix

427 – 436

10

Helix

437 – 441

5

Sequences

	Sequence		Length	Mass (Da)
	P47039 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: AAEA86D7AD24F924	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

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. , 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: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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].
[4]	"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].
[5]	"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.
[6]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z49335 Genomic DNA. Translation: CAA89351.1.
BK006943 Genomic DNA. Translation: DAA08738.1.

PIR

S56832.

RefSeq

NP_012475.1. NM_001181493.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P47039.

SMR

P47039. Positions 18-444.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6723N.

IntAct

P47039. 10 interactions.

MINT

MINT-658286.

STRING

P47039.

Proteomic databases

PeptideAtlas

P47039.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJL060W; YJL060W; YJL060W.

GeneID

853386.

KEGG

sce:YJL060W.

NMPDR

fig|4932.3.peg.3447.

Organism-specific databases

CYGD

YJL060w.

SGD

S000003596. BNA3.

Phylogenomic databases

eggNOG

fuNOG04782.

GeneTree

EFGT00050000001332.

HOGENOM

HBG645860.

OMA

CANSIND.

OrthoDB

EOG4WHCV4.

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.

KO

K14264.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00753. ACCSYNTHASE.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

973849.

Entry information

Entry name

BNA3_YEAST

Accession

Primary (citable) accession number: P47039
Secondary accession number(s): D6VWC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	December 14, 2011
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program