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Protein

Aromatic/aminoadipate aminotransferase 1

Gene

ARO8

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

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.5 Publications

Catalytic activityi

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.

Cofactori

Pathwayi: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-phenylalanine from phenylpyruvate (ArAT route).
Proteins known to be involved in this subpathway in this organism are:
  1. Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-phenylalanine from phenylpyruvate (ArAT route), the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-tyrosine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-tyrosine from (4-hydroxyphenyl)pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-tyrosine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tyrosine from (4-hydroxyphenyl)pyruvate, the pathway L-tyrosine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 6 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (MRI1)
  2. Methylthioribulose-1-phosphate dehydratase (MDE1)
  3. Enolase-phosphatase E1 (UTR4)
  4. Enolase-phosphatase E1 (UTR4)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (ADI1)
  6. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Aromatic amino acid aminotransferase 2 (ARO9), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Pathwayi: L-lysine biosynthesis via AAA pathway

This protein is involved in step 5 of the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Homocitrate synthase, cytosolic isozyme (LYS20), Homocitrate synthase, mitochondrial (LYS21)
  2. Homocitrate dehydratase, mitochondrial (ACO2)
  3. Homoaconitase, mitochondrial (LYS4)
  4. Homoisocitrate dehydrogenase, mitochondrial (LYS12)
  5. Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate, the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11841.
YEAST:YGL202W-MONOMER.
BRENDAi2.6.1.57. 984.
ReactomeiR-SCE-71064. Lysine catabolism.
R-SCE-71240. Tryptophan catabolism.
UniPathwayiUPA00033; UER00031.
UPA00121; UER00347.
UPA00122; UER00350.
UPA00904; UER00879.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ARO8
Ordered Locus Names:YGL202W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL202W.
SGDiS000003170. ARO8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500Aromatic/aminoadipate aminotransferase 1PRO_0000064678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53090.
PeptideAtlasiP53090.

PTM databases

iPTMnetiP53090.

Interactioni

Protein-protein interaction databases

BioGridi33055. 51 interactions.
DIPiDIP-983N.
IntActiP53090. 1 interaction.
MINTiMINT-4486305.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Helixi15 – 195Combined sources
Helixi24 – 296Combined sources
Turni30 – 334Combined sources
Beta strandi37 – 393Combined sources
Helixi47 – 493Combined sources
Beta strandi53 – 597Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 825Combined sources
Helixi89 – 913Combined sources
Helixi99 – 1024Combined sources
Helixi112 – 12514Combined sources
Beta strandi133 – 1397Combined sources
Helixi141 – 15212Combined sources
Beta strandi158 – 1647Combined sources
Helixi167 – 1759Combined sources
Beta strandi179 – 1835Combined sources
Helixi192 – 2009Combined sources
Beta strandi211 – 2144Combined sources
Turni220 – 2223Combined sources
Helixi228 – 24114Combined sources
Beta strandi244 – 2485Combined sources
Helixi252 – 2543Combined sources
Helixi263 – 2719Combined sources
Helixi277 – 2837Combined sources
Helixi288 – 2914Combined sources
Beta strandi293 – 2953Combined sources
Beta strandi297 – 3037Combined sources
Turni304 – 3074Combined sources
Helixi309 – 3113Combined sources
Beta strandi314 – 3196Combined sources
Helixi320 – 33112Combined sources
Turni332 – 3343Combined sources
Helixi339 – 38244Combined sources
Beta strandi395 – 40511Combined sources
Helixi406 – 4083Combined sources
Turni410 – 4189Combined sources
Helixi420 – 43314Combined sources
Helixi441 – 4444Combined sources
Helixi456 – 4594Combined sources
Beta strandi466 – 47611Combined sources
Helixi478 – 49518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JE5X-ray1.91A/B/C/D1-500[»]
ProteinModelPortaliP53090.
SMRiP53090. Positions 2-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000004594.
HOGENOMiHOG000223057.
InParanoidiP53090.
KOiK00838.
OMAiGMFHWIE.
OrthoDBiEOG7M6DHB.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
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. 2 hits.

Sequencei

Sequence statusi: Complete.

P53090-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLPESKDFS YLFSDETNAR KPSPLKTCIH LFQDPNIIFL GGGLPLKDYF
60 70 80 90 100
PWDNLSVDSP KPPFPQGIGA PIDEQNCIKY TVNKDYADKS ANPSNDIPLS
110 120 130 140 150
RALQYGFSAG QPELLNFIRD HTKIIHDLKY KDWDVLATAG NTNAWESTLR
160 170 180 190 200
VFCNRGDVIL VEAHSFSSSL ASAEAQGVIT FPVPIDADGI IPEKLAKVME
210 220 230 240 250
NWTPGAPKPK LLYTIPTGQN PTGTSIADHR KEAIYKIAQK YDFLIVEDEP
260 270 280 290 300
YYFLQMNPYI KDLKEREKAQ SSPKQDHDEF LKSLANTFLS LDTEGRVIRM
310 320 330 340 350
DSFSKVLAPG TRLGWITGSS KILKPYLSLH EMTIQAPAGF TQVLVNATLS
360 370 380 390 400
RWGQKGYLDW LLGLRHEYTL KRDCAIDALY KYLPQSDAFV INPPIAGMFF
410 420 430 440 450
TVNIDASVHP EFKTKYNSDP YQLEQSLYHK VVERGVLVVP GSWFKSEGET
460 470 480 490 500
EPPQPAESKE VSNPNIIFFR GTYAAVSPEK LTEGLKRLGD TLYEEFGISK
Length:500
Mass (Da):56,178
Last modified:October 1, 1996 - v1
Checksum:iD0D111640D2C560D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13624 Genomic DNA. Translation: CAA73946.1.
Z72724 Genomic DNA. Translation: CAA96914.1.
AY692962 Genomic DNA. Translation: AAT92981.1.
BK006941 Genomic DNA. Translation: DAA07913.1.
PIRiS64220.
RefSeqiNP_011313.1. NM_001181067.1.

Genome annotation databases

EnsemblFungiiYGL202W; YGL202W; YGL202W.
GeneIDi852672.
KEGGisce:YGL202W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13624 Genomic DNA. Translation: CAA73946.1.
Z72724 Genomic DNA. Translation: CAA96914.1.
AY692962 Genomic DNA. Translation: AAT92981.1.
BK006941 Genomic DNA. Translation: DAA07913.1.
PIRiS64220.
RefSeqiNP_011313.1. NM_001181067.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JE5X-ray1.91A/B/C/D1-500[»]
ProteinModelPortaliP53090.
SMRiP53090. Positions 2-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33055. 51 interactions.
DIPiDIP-983N.
IntActiP53090. 1 interaction.
MINTiMINT-4486305.

PTM databases

iPTMnetiP53090.

Proteomic databases

MaxQBiP53090.
PeptideAtlasiP53090.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL202W; YGL202W; YGL202W.
GeneIDi852672.
KEGGisce:YGL202W.

Organism-specific databases

EuPathDBiFungiDB:YGL202W.
SGDiS000003170. ARO8.

Phylogenomic databases

GeneTreeiENSGT00390000004594.
HOGENOMiHOG000223057.
InParanoidiP53090.
KOiK00838.
OMAiGMFHWIE.
OrthoDBiEOG7M6DHB.

Enzyme and pathway databases

UniPathwayiUPA00033; UER00031.
UPA00121; UER00347.
UPA00122; UER00350.
UPA00904; UER00879.
BioCyciMetaCyc:MONOMER-11841.
YEAST:YGL202W-MONOMER.
BRENDAi2.6.1.57. 984.
ReactomeiR-SCE-71064. Lysine catabolism.
R-SCE-71240. Tryptophan catabolism.

Miscellaneous databases

NextBioi971973.
PROiP53090.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
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. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARO8_YEAST
AccessioniPrimary (citable) accession number: P53090
Secondary accession number(s): D6VTV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 130 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 1770 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.