P53090 (ARO8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aromatic/aminoadipate aminotransferase 1

Alternative name(s):
2-aminoadipate aminotransferase
EC=2.6.1.39
2-aminoadipate transaminase
Alpha-aminoadipate aminotransferase
Short name=AadAT
Aromatic amino acid aminotransferase 1
EC=2.6.1.57
Aromatic amino acid aminotransferase I
Aromatic amino acid-requiring protein 8

Gene names

Name:	ARO8
Ordered Locus Names:	YGL202W

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	Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from phenylpyruvate (ArAT route): step 1/1. Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from (4-hydroxyphenyl)pyruvate: step 1/1. Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 6/6. Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 4/4.
Subcellular location	Cytoplasm Ref.7.
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 process Inferred 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 activity Inferred from electronic annotation. Source: EC aromatic-amino-acid:2-oxoglutarate aminotransferase 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 – 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

	Sequence		Length	Mass (Da)
	P53090 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D0D111640D2C560D	FASTA	500	56,178
	10 20 30 40 50 60 MTLPESKDFS YLFSDETNAR KPSPLKTCIH LFQDPNIIFL GGGLPLKDYF PWDNLSVDSP 70 80 90 100 110 120 KPPFPQGIGA PIDEQNCIKY TVNKDYADKS ANPSNDIPLS RALQYGFSAG QPELLNFIRD 130 140 150 160 170 180 HTKIIHDLKY KDWDVLATAG NTNAWESTLR VFCNRGDVIL VEAHSFSSSL ASAEAQGVIT 190 200 210 220 230 240 FPVPIDADGI IPEKLAKVME NWTPGAPKPK LLYTIPTGQN PTGTSIADHR KEAIYKIAQK 250 260 270 280 290 300 YDFLIVEDEP YYFLQMNPYI KDLKEREKAQ SSPKQDHDEF LKSLANTFLS LDTEGRVIRM 310 320 330 340 350 360 DSFSKVLAPG TRLGWITGSS KILKPYLSLH EMTIQAPAGF TQVLVNATLS RWGQKGYLDW 370 380 390 400 410 420 LLGLRHEYTL KRDCAIDALY KYLPQSDAFV INPPIAGMFF TVNIDASVHP EFKTKYNSDP 430 440 450 460 470 480 YQLEQSLYHK VVERGVLVVP GSWFKSEGET EPPQPAESKE VSNPNIIFFR GTYAAVSPEK 490 500 LTEGLKRLGD TLYEEFGISK

References

	« Hide 'large scale' referencesShow '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. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., 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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., 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

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program