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Protein

Aspartate aminotransferase, cytoplasmic

Gene

AAT2

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

Plays a key role in amino acid metabolism.

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.3 Publications

Cofactori

pyridoxal 5'-phosphate2 Publications

Kineticsi

  1. KM=0.11 mM for L-aspartate1 Publication
  2. KM=20 mM for L-glutamate1 Publication
  3. KM=0.006 mM for oxaloacetate1 Publication
  4. KM=0.16 mM for 2-oxoglutarate1 Publication

    pH dependencei

    Optimum pH is 8-9.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei38 – 381Aspartate; via amide nitrogen1 Publication
    Binding sitei135 – 1351Aspartate1 Publication
    Binding sitei188 – 1881Aspartate1 Publication
    Binding sitei387 – 3871Aspartate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • 2-oxoglutarate metabolic process Source: UniProtKB
    • aspartate biosynthetic process Source: SGD
    • aspartate metabolic process Source: UniProtKB
    • glutamate metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13013.
    YEAST:YLR027C-MONOMER.
    ReactomeiREACT_286539. Gluconeogenesis.
    REACT_288999. Amino acid synthesis and interconversion (transamination).
    REACT_350157. Methionine salvage pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate aminotransferase, cytoplasmic (EC:2.6.1.1)
    Alternative name(s):
    Transaminase A
    Gene namesi
    Name:AAT2
    Synonyms:ASP5
    Ordered Locus Names:YLR027C
    ORF Names:L1746
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XII

    Organism-specific databases

    EuPathDBiFungiDB:YLR027C.
    SGDiS000004017. AAT2.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: SGD
    • peroxisome Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 418417Aspartate aminotransferase, cytoplasmicPRO_0000123875Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei255 – 2551N6-(pyridoxal phosphate)lysine1 Publication
    Modified residuei389 – 3891Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23542.
    PaxDbiP23542.
    PeptideAtlasiP23542.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi31301. 178 interactions.
    DIPiDIP-2897N.
    IntActiP23542. 12 interactions.
    MINTiMINT-701237.
    STRINGi4932.YLR027C.

    Structurei

    Secondary structure

    1
    418
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 86Combined sources
    Helixi18 – 258Combined sources
    Helixi51 – 6111Combined sources
    Helixi77 – 8812Combined sources
    Helixi93 – 964Combined sources
    Beta strandi100 – 1067Combined sources
    Helixi107 – 12216Combined sources
    Beta strandi128 – 1336Combined sources
    Helixi138 – 1436Combined sources
    Turni144 – 1463Combined sources
    Beta strandi149 – 1535Combined sources
    Turni157 – 1604Combined sources
    Helixi164 – 17310Combined sources
    Beta strandi179 – 1835Combined sources
    Turni188 – 1903Combined sources
    Helixi196 – 20813Combined sources
    Beta strandi212 – 2187Combined sources
    Turni220 – 2223Combined sources
    Beta strandi223 – 2253Combined sources
    Helixi227 – 2304Combined sources
    Helixi232 – 2409Combined sources
    Turni241 – 2444Combined sources
    Beta strandi247 – 2526Combined sources
    Turni254 – 2563Combined sources
    Helixi260 – 2623Combined sources
    Beta strandi264 – 2707Combined sources
    Helixi277 – 29317Combined sources
    Turni294 – 2963Combined sources
    Helixi301 – 31212Combined sources
    Helixi314 – 34532Combined sources
    Helixi353 – 3564Combined sources
    Beta strandi359 – 3635Combined sources
    Helixi368 – 37811Combined sources
    Beta strandi386 – 3894Combined sources
    Helixi390 – 3923Combined sources
    Turni395 – 3973Combined sources
    Helixi398 – 41114Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YAAX-ray2.05A/B/C/D2-412[»]
    ProteinModelPortaliP23542.
    SMRiP23542. Positions 2-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23542.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1448.
    GeneTreeiENSGT00390000014081.
    HOGENOMiHOG000185898.
    InParanoidiP23542.
    KOiK14454.
    OMAiDSAIWIG.
    OrthoDBiEOG793BHW.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PANTHERiPTHR11879. PTHR11879. 1 hit.
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    PRINTSiPR00799. TRANSAMINASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P23542-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSATLFNNIE LLPPDALFGI KQRYGQDQRA TKVDLGIGAY RDDNGKPWVL
    60 70 80 90 100
    PSVKAAEKLI HNDSSYNHEY LGITGLPSLT SNAAKIIFGT QSDAFQEDRV
    110 120 130 140 150
    ISVQSLSGTG ALHISAKFFS KFFPDKLVYL SKPTWANHMA IFENQGLKTA
    160 170 180 190 200
    TYPYWANETK SLDLNGFLNA IQKAPEGSIF VLHSCAHNPT GLDPTSEQWV
    210 220 230 240 250
    QIVDAIASKN HIALFDTAYQ GFATGDLDKD AYAVRLGVEK LSTVSPVFVC
    260 270 280 290 300
    QSFAKNAGMY GERVGCFHLA LTKQAQNKTI KPAVTSQLAK IIRSEVSNPP
    310 320 330 340 350
    AYGAKIVAKL LETPELTEQW HKDMVTMSSR ITKMRHALRD HLVKLGTPGN
    360 370 380 390 400
    WDHIVNQCGM FSFTGLTPQM VKRLEETHAV YLVASGRASI AGLNQGNVEY
    410
    VAKAIDEVVR FYTIEAKL
    Length:418
    Mass (Da):46,058
    Last modified:January 23, 2007 - v3
    Checksum:iD25F40F6C6DD2B33
    GO

    Sequence cautioni

    The sequence CAA97550.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951F → L AA sequence (PubMed:2199266).Curated
    Sequence conflicti95 – 951F → L AA sequence (PubMed:1859361).Curated
    Sequence conflicti413 – 4142TI → AT AA sequence (PubMed:2199266).Curated
    Sequence conflicti413 – 4142TI → AT AA sequence (PubMed:1859361).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z73199 Genomic DNA. Translation: CAA97550.1. Different initiation.
    BK006945 Genomic DNA. Translation: DAA09345.1.
    PIRiS64854.
    RefSeqiNP_013127.2. NM_001181914.1.

    Genome annotation databases

    EnsemblFungiiYLR027C; YLR027C; YLR027C.
    GeneIDi850714.
    KEGGisce:YLR027C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z73199 Genomic DNA. Translation: CAA97550.1. Different initiation.
    BK006945 Genomic DNA. Translation: DAA09345.1.
    PIRiS64854.
    RefSeqiNP_013127.2. NM_001181914.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YAAX-ray2.05A/B/C/D2-412[»]
    ProteinModelPortaliP23542.
    SMRiP23542. Positions 2-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31301. 178 interactions.
    DIPiDIP-2897N.
    IntActiP23542. 12 interactions.
    MINTiMINT-701237.
    STRINGi4932.YLR027C.

    Proteomic databases

    MaxQBiP23542.
    PaxDbiP23542.
    PeptideAtlasiP23542.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYLR027C; YLR027C; YLR027C.
    GeneIDi850714.
    KEGGisce:YLR027C.

    Organism-specific databases

    EuPathDBiFungiDB:YLR027C.
    SGDiS000004017. AAT2.

    Phylogenomic databases

    eggNOGiCOG1448.
    GeneTreeiENSGT00390000014081.
    HOGENOMiHOG000185898.
    InParanoidiP23542.
    KOiK14454.
    OMAiDSAIWIG.
    OrthoDBiEOG793BHW.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13013.
    YEAST:YLR027C-MONOMER.
    ReactomeiREACT_286539. Gluconeogenesis.
    REACT_288999. Amino acid synthesis and interconversion (transamination).
    REACT_350157. Methionine salvage pathway.

    Miscellaneous databases

    EvolutionaryTraceiP23542.
    NextBioi966778.
    PROiP23542.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PANTHERiPTHR11879. PTHR11879. 1 hit.
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    PRINTSiPR00799. TRANSAMINASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Amino acid sequences of aspartate aminotransferases: the cytosolic isoenzymes from yeast and from human liver."
      Cronin V.B., Doyle J.M., Doonan S.
      Biochem. Soc. Trans. 18:256-256(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-418.
    4. "The amino acid sequence of the aspartate aminotransferase from baker's yeast (Saccharomyces cerevisiae)."
      Cronin V.B., Maras B., Barra D., Doonan S.
      Biochem. J. 277:335-340(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-418, ACETYLATION AT SER-2, ENZYME ACTIVITY.
    5. "Aspartate: 2-oxoglutarate aminotransferase from bakers' yeast: crystallization and characterization."
      Yagi T., Kagamiyama H., Nozaki M.
      J. Biochem. 92:35-43(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    6. "Cytosolic aspartate aminotransferase encoded by the AAT2 gene is targeted to the peroxisomes in oleate-grown Saccharomyces cerevisiae."
      Verleur N., Elgersma Y., Van Roermund C.W., Tabak H.F., Wanders R.J.
      Eur. J. Biochem. 247:972-980(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase."
      Jeffery C.J., Barry T., Doonan S., Petsko G.A., Ringe D.
      Protein Sci. 7:1380-1387(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH PYRODOXAL PHOSPHATE AND MALEIC ACID, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-255, SUBUNIT.

    Entry informationi

    Entry nameiAATC_YEAST
    AccessioniPrimary (citable) accession number: P23542
    Secondary accession number(s): D6VY29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 153 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
    Present with 7700 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3

    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 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.