P53090 (ARO8_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 91.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Aromatic/aminoadipate aminotransferase 1 | ||||
| Gene names |
| ||||
| 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 | 500 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Responsible for phenylalanine and tyrosine biosynthesis. Active with glutamate, phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors. Also active with methionine, alpha-aminoadipate and leucine as amino donors when phenylpyruvate is the amino acceptor and in the reverse reactions with the corresponding oxo acids and phenylalanine as amino donor. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the formation of alpha-aminoadipate from alpha-ketoadipate in the lysine biosyntheic pathway. Ref.1 Ref.5 Ref.6 Ref.10 Ref.12 |
| Catalytic activity | An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate. An aromatic amino acid + 4-(methylthio)-2-oxobutanoate = an aromatic oxo acid + L-methionine. L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | |
| Subcellular location | |
| Miscellaneous | Present with 1770 molecules/cell in log phase SD medium. Ref.8 |
| Sequence similarities | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | aromatic amino acid family metabolic process Inferred from mutant phenotype Ref.1. Source: SGD biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from direct assay Ref.7. Source: SGD |
| Molecular function | 2-aminoadipate transaminase activity Inferred from direct assay. Source: SGD L-phenylalanine:2-oxoglutarate aminotransferase activityInferred from electronic annotation. Source: EC aromatic-amino-acid:2-oxoglutarate aminotransferase activityInferred from direct assay Ref.6. Source: SGD pyridoxal phosphate bindingInferred 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 – 500 | 500 | Aromatic/aminoadipate aminotransferase 1 | PRO_0000064678 | |||||
Amino acid modifications | |||||||||
| Modified residue | 56 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 100 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 271 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 272 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 477 | 1 | Phosphoserine Ref.11 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily." Iraqui I., Vissers S., Cartiaux M., Urrestarazu A. Mol. Gen. Genet. 257:238-248(1998) [PubMed: 9491083] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: Sigma 1278B. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K.Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [3] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [4] | "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J.Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [5] | "Tryptophan degradation in Saccharomyces cerevisiae: characterization of two aromatic aminotransferases." Kradolfer P., Niederberger P., Hutter R. Arch. Microbiol. 133:242-248(1982) [PubMed: 6763508] [Abstract] Cited for: FUNCTION. |
| [6] | "Phenylalanine- and tyrosine-auxotrophic mutants of Saccharomyces cerevisiae impaired in transamination." Urrestarazu A., Vissers S., Iraqui I., Grenson M. Mol. Gen. Genet. 257:230-237(1998) [PubMed: 9491082] [Abstract] Cited for: FUNCTION. |
| [7] | "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]. |
| [8] | "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]. |
| [9] | "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, MASS SPECTROMETRY. |
| [10] | "A complete inventory of all enzymes in the eukaryotic methionine salvage pathway." Pirkov I., Norbeck J., Gustafsson L., Albers E. FEBS J. 275:4111-4120(2008) [PubMed: 18625006] [Abstract] Cited for: FUNCTION. |
| [11] | "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-56; SER-100; SER-272 AND SER-477, MASS SPECTROMETRY. |
| [12] | "Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae." Karsten W.E., Reyes Z.L., Bobyk K.D., Cook P.F., Chooback L. Arch. Biochem. Biophys. 516:67-74(2011) [PubMed: 21982920] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y13624 Genomic DNA. Translation: CAA73946.1. Z72724 Genomic DNA. Translation: CAA96914.1. AY692962 Genomic DNA. Translation: AAT92981.1. BK006941 Genomic DNA. Translation: DAA07913.1. |
| PIR | S64220. |
| RefSeq | NP_011313.1. NM_001181067.1. |
3D structure databases | |
| ProteinModelPortal | P53090. |
| SMR | P53090. Positions 8-496. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-983N. |
| IntAct | P53090. 86 interactions. |
| STRING | P53090. |
Proteomic databases | |
| PeptideAtlas | P53090. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YGL202W; YGL202W; YGL202W. |
| GeneID | 852672. |
| KEGG | sce:YGL202W. |
| NMPDR | fig|4932.3.peg.2416. |
Organism-specific databases | |
| CYGD | YGL202w. |
| SGD | S000003170. ARO8. |
Phylogenomic databases | |
| eggNOG | fuNOG04028. |
| GeneTree | EFGT00050000001374. |
| HOGENOM | HBG752297. |
| OMA | LYTICTG. |
| OrthoDB | EOG4SBJ68. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-11841. |
| BRENDA | 2.6.1.57. 984. |
Gene expression databases | |
| ArrayExpress | P53090. |
| Genevestigator | P53090. |
| GermOnline | YGL202W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR004839. Aminotransferase_I/II. 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 | K00838. |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| ProtoNet | Search... |
Other | |
| NextBio | 971973. |
Entry information
| Entry name | ARO8_YEAST | ||||||||
| Accession | Primary (citable) accession number: P53090 Secondary accession number(s): D6VTV2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome VII Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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