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P23542

- AATC_YEAST

UniProt

P23542 - AATC_YEAST

Protein

Aspartate aminotransferase, cytoplasmic

Gene

AAT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Plays a key role in amino acid metabolism.

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.2 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 nitrogen
    Binding sitei135 – 1351Aspartate
    Binding sitei188 – 1881Aspartate
    Binding sitei387 – 3871Aspartate

    GO - Molecular functioni

    1. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
    2. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
    3. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. aspartate biosynthetic process Source: SGD
    3. aspartate metabolic process Source: UniProtKB
    4. glutamate metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13013.
    YEAST:YLR027C-MONOMER.
    ReactomeiREACT_189018. 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: Chromosome XII

    Organism-specific databases

    SGDiS000004017. AAT2.

    Subcellular locationi

    Cytoplasm 1 Publication. Peroxisome 1 Publication
    Note: Targeted to peroxisomes in cells grown in oleate.

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. peroxisome Source: SGD

    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)lysine
    Modified residuei389 – 3891Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23542.
    PaxDbiP23542.
    PeptideAtlasiP23542.

    Expressioni

    Gene expression databases

    GenevestigatoriP23542.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi31301. 177 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 – 86
    Helixi18 – 258
    Helixi51 – 6111
    Helixi77 – 8812
    Helixi93 – 964
    Beta strandi100 – 1067
    Helixi107 – 12216
    Beta strandi128 – 1336
    Helixi138 – 1436
    Turni144 – 1463
    Beta strandi149 – 1535
    Turni157 – 1604
    Helixi164 – 17310
    Beta strandi179 – 1835
    Turni188 – 1903
    Helixi196 – 20813
    Beta strandi212 – 2187
    Turni220 – 2223
    Beta strandi223 – 2253
    Helixi227 – 2304
    Helixi232 – 2409
    Turni241 – 2444
    Beta strandi247 – 2526
    Turni254 – 2563
    Helixi260 – 2623
    Beta strandi264 – 2707
    Helixi277 – 29317
    Turni294 – 2963
    Helixi301 – 31212
    Helixi314 – 34532
    Helixi353 – 3564
    Beta strandi359 – 3635
    Helixi368 – 37811
    Beta strandi386 – 3894
    Helixi390 – 3923
    Turni395 – 3973
    Helixi398 – 41114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK14454.
    OMAiSSRIRQM.
    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

    MSATLFNNIE LLPPDALFGI KQRYGQDQRA TKVDLGIGAY RDDNGKPWVL    50
    PSVKAAEKLI HNDSSYNHEY LGITGLPSLT SNAAKIIFGT QSDAFQEDRV 100
    ISVQSLSGTG ALHISAKFFS KFFPDKLVYL SKPTWANHMA IFENQGLKTA 150
    TYPYWANETK SLDLNGFLNA IQKAPEGSIF VLHSCAHNPT GLDPTSEQWV 200
    QIVDAIASKN HIALFDTAYQ GFATGDLDKD AYAVRLGVEK LSTVSPVFVC 250
    QSFAKNAGMY GERVGCFHLA LTKQAQNKTI KPAVTSQLAK IIRSEVSNPP 300
    AYGAKIVAKL LETPELTEQW HKDMVTMSSR ITKMRHALRD HLVKLGTPGN 350
    WDHIVNQCGM FSFTGLTPQM VKRLEETHAV YLVASGRASI AGLNQGNVEY 400
    VAKAIDEVVR FYTIEAKL 418
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z73199 Genomic DNA. Translation: CAA97550.1 . Different initiation.
    BK006945 Genomic DNA. Translation: DAA09345.1 .
    PIRi S64854.
    RefSeqi NP_013127.2. NM_001181914.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YAA X-ray 2.05 A/B/C/D 2-412 [» ]
    ProteinModelPortali P23542.
    SMRi P23542. Positions 2-412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31301. 177 interactions.
    DIPi DIP-2897N.
    IntActi P23542. 12 interactions.
    MINTi MINT-701237.
    STRINGi 4932.YLR027C.

    Proteomic databases

    MaxQBi P23542.
    PaxDbi P23542.
    PeptideAtlasi P23542.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR027C ; YLR027C ; YLR027C .
    GeneIDi 850714.
    KEGGi sce:YLR027C.

    Organism-specific databases

    SGDi S000004017. AAT2.

    Phylogenomic databases

    eggNOGi COG1448.
    GeneTreei ENSGT00390000014081.
    HOGENOMi HOG000185898.
    KOi K14454.
    OMAi SSRIRQM.
    OrthoDBi EOG793BHW.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13013.
    YEAST:YLR027C-MONOMER.
    Reactomei REACT_189018. Methionine salvage pathway.

    Miscellaneous databases

    EvolutionaryTracei P23542.
    NextBioi 966778.
    PROi P23542.

    Gene expression databases

    Genevestigatori P23542.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view ]
    PANTHERi PTHR11879. PTHR11879. 1 hit.
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00799. TRANSAMINASE.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    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: October 1, 2014
    This is version 146 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