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P00509

- AAT_ECOLI

UniProt

P00509 - AAT_ECOLI

Protein

Aspartate aminotransferase

Gene

aspC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.1 Publication

    Cofactori

    Pyridoxal phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341Aspartate; via amide nitrogen
    Binding sitei130 – 1301Aspartate
    Binding sitei183 – 1831Aspartate
    Binding sitei374 – 3741Aspartate

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. L-aspartate:2-oxoglutarate aminotransferase activity Source: EcoliWiki
    3. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
    4. L-tyrosine:2-oxoglutarate aminotransferase activity Source: EcoliWiki
    5. pyridoxal phosphate binding Source: EcoliWiki

    GO - Biological processi

    1. L-phenylalanine biosynthetic process Source: EcoliWiki
    2. L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Source: EcoCyc

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:ASPAMINOTRANS-MONOMER.
    ECOL316407:JW0911-MONOMER.
    MetaCyc:ASPAMINOTRANS-MONOMER.
    BRENDAi2.6.1.1. 2026.
    SABIO-RKP00509.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate aminotransferase (EC:2.6.1.1)
    Short name:
    AspAT
    Alternative name(s):
    Transaminase A
    Gene namesi
    Name:aspC
    Ordered Locus Names:b0928, JW0911
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10096. aspC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651Y → F or S: Slight changes in activity. 1 Publication
    Mutagenesisi133 – 1331H → A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. 1 Publication
    Mutagenesisi133 – 1331H → N: Decreases to 60% in maximum rate of the overall reactions in both directions. 1 Publication
    Mutagenesisi280 – 2801R → V: Reduces first-order rate constant over 25000-fold. 1 Publication
    Mutagenesisi374 – 3741R → A: Reduces first-order rate constant about 10000-fold. 2 Publications
    Mutagenesisi374 – 3741R → F or Y: Second-order rate constants are reduced by >5 orders of magnitude. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396Aspartate aminotransferasePRO_0000123838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461N6-(pyridoxal phosphate)lysine1 Publication

    Proteomic databases

    PaxDbiP00509.
    PRIDEiP00509.

    2D gel databases

    SWISS-2DPAGEP00509.

    Expressioni

    Gene expression databases

    GenevestigatoriP00509.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-907474,EBI-907474

    Protein-protein interaction databases

    DIPiDIP-9181N.
    IntActiP00509. 4 interactions.
    STRINGi511145.b0928.

    Structurei

    Secondary structure

    1
    396
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2 – 43
    Helixi12 – 2211
    Beta strandi29 – 324
    Beta strandi33 – 353
    Turni39 – 413
    Helixi47 – 5913
    Helixi72 – 8312
    Helixi88 – 914
    Beta strandi95 – 1017
    Helixi102 – 11716
    Beta strandi122 – 1287
    Helixi132 – 1398
    Beta strandi143 – 1486
    Turni152 – 1554
    Helixi159 – 1668
    Beta strandi174 – 1785
    Beta strandi179 – 1813
    Turni183 – 1853
    Helixi191 – 20414
    Beta strandi207 – 2137
    Beta strandi217 – 2193
    Helixi221 – 2244
    Helixi226 – 2349
    Beta strandi238 – 2436
    Turni245 – 2495
    Helixi251 – 2533
    Beta strandi256 – 2616
    Helixi265 – 28016
    Turni281 – 2833
    Helixi288 – 29811
    Helixi301 – 33131
    Helixi340 – 3434
    Beta strandi346 – 3505
    Helixi355 – 36511
    Beta strandi367 – 3693
    Turni371 – 3733
    Beta strandi374 – 3763
    Helixi377 – 3793
    Turni382 – 3843
    Helixi385 – 39511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AAMX-ray2.80A1-396[»]
    1AAWX-ray2.40A1-396[»]
    1AHEX-ray2.30A/B1-396[»]
    1AHFX-ray2.30A/B1-396[»]
    1AHGX-ray2.50A/B1-396[»]
    1AHXX-ray2.00A/B1-396[»]
    1AHYX-ray2.30A/B1-396[»]
    1AIAX-ray2.20A/B1-396[»]
    1AIBX-ray2.80A/B1-396[»]
    1AICX-ray2.40A/B1-396[»]
    1AMQX-ray2.20A1-396[»]
    1AMRX-ray2.10A1-396[»]
    1AMSX-ray2.70A1-396[»]
    1ARGX-ray2.20A/B1-396[»]
    1ARHX-ray2.30A/B1-396[»]
    1ARIX-ray2.30A/B1-396[»]
    1ARSX-ray1.80A1-396[»]
    1ARTX-ray1.80A1-396[»]
    1ASAX-ray2.40A1-396[»]
    1ASBX-ray2.60A1-396[»]
    1ASCX-ray2.40A1-396[»]
    1ASDX-ray2.20A1-396[»]
    1ASEX-ray2.50A1-396[»]
    1ASFX-ray2.80A1-396[»]
    1ASGX-ray2.80A1-396[»]
    1ASLX-ray2.60A/B1-396[»]
    1ASMX-ray2.35A/B1-396[»]
    1ASNX-ray2.50A/B1-396[»]
    1B4XX-ray2.45A1-396[»]
    1BQAX-ray2.10A/B1-396[»]
    1BQDX-ray2.10A/B1-396[»]
    1C9CX-ray2.40A1-396[»]
    1CQ6X-ray2.70A1-396[»]
    1CQ7X-ray2.40A1-396[»]
    1CQ8X-ray2.40A1-396[»]
    1CZCX-ray2.50A1-396[»]
    1CZEX-ray2.40A1-396[»]
    1G4VX-ray2.00A1-396[»]
    1G4XX-ray2.20A1-396[»]
    1G7WX-ray2.20A1-396[»]
    1G7XX-ray2.20A1-396[»]
    1IX6X-ray2.20A1-396[»]
    1IX7X-ray2.20A1-396[»]
    1IX8X-ray2.20A1-396[»]
    1QIRX-ray2.20A1-396[»]
    1QISX-ray1.90A1-396[»]
    1QITX-ray1.90A1-396[»]
    1SPAX-ray2.00A1-396[»]
    1TOEX-ray2.00A1-388[»]
    1TOGX-ray2.31A/B1-388[»]
    1TOIX-ray1.90A1-388[»]
    1TOJX-ray1.90A1-388[»]
    1TOKX-ray1.85A/B1-388[»]
    1X28X-ray2.40A/B1-396[»]
    1X29X-ray2.20A/B1-396[»]
    1X2AX-ray2.20A/B1-396[»]
    1YOOX-ray2.40A1-396[»]
    2AATX-ray2.80A1-396[»]
    2D5YX-ray1.98A1-396[»]
    2D61X-ray2.01A1-396[»]
    2D63X-ray2.05A1-396[»]
    2D64X-ray2.05A1-396[»]
    2D65X-ray2.30A1-396[»]
    2D66X-ray2.18A1-396[»]
    2D7YX-ray2.66A1-396[»]
    2D7ZX-ray2.65A1-396[»]
    2Q7WX-ray1.40A1-396[»]
    2QA3X-ray1.75A1-396[»]
    2QB2X-ray1.70A1-396[»]
    2QB3X-ray1.45A1-396[»]
    2QBTX-ray1.75A1-396[»]
    3AATX-ray2.80A1-396[»]
    3QN6X-ray1.79A1-396[»]
    3QPGX-ray1.79A1-396[»]
    3ZZJX-ray2.50A1-396[»]
    3ZZKX-ray1.78A1-396[»]
    4A00X-ray2.34A1-396[»]
    4DBCX-ray1.50A1-396[»]
    4F5FX-ray2.25A/B2-396[»]
    4F5GX-ray1.67A/B2-396[»]
    4F5HX-ray1.60A/B2-396[»]
    4F5IX-ray2.20A/B2-396[»]
    4F5JX-ray1.95A/B2-396[»]
    4F5KX-ray2.20A/B2-396[»]
    4F5LX-ray1.40A/B2-396[»]
    4F5MX-ray1.65A/B2-396[»]
    5EAAX-ray2.40A1-396[»]
    ProteinModelPortaliP00509.
    SMRiP00509. Positions 1-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00509.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1448.
    HOGENOMiHOG000185899.
    KOiK00813.
    OMAiRVGACTI.
    OrthoDBiEOG6C2WBK.
    PhylomeDBiP00509.

    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.

    P00509-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK    50
    KAEQYLLENE TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT 100
    PGGTGALRVA ADFLAKNTSV KRVWVSNPSW PNHKSVFNSA GLEVREYAYY 150
    DAENHTLDFD ALINSLNEAQ AGDVVLFHGC CHNPTGIDPT LEQWQTLAQL 200
    SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV ASSYSKNFGL 250
    YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN 300
    DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF 350
    SGLTKEQVLR LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL 396
    Length:396
    Mass (Da):43,573
    Last modified:July 21, 1986 - v1
    Checksum:i9F0437E76DD4FC0F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03629 Genomic DNA. Translation: CAA27279.1.
    X05904 Genomic DNA. Translation: CAA29333.1.
    U00096 Genomic DNA. Translation: AAC74014.1.
    AP009048 Genomic DNA. Translation: BAA35674.1.
    PIRiA00598. XNECD.
    RefSeqiNP_415448.1. NC_000913.3.
    YP_489200.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74014; AAC74014; b0928.
    BAA35674; BAA35674; BAA35674.
    GeneIDi12931027.
    945553.
    KEGGiecj:Y75_p0900.
    eco:b0928.
    PATRICi32117069. VBIEscCol129921_0959.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03629 Genomic DNA. Translation: CAA27279.1 .
    X05904 Genomic DNA. Translation: CAA29333.1 .
    U00096 Genomic DNA. Translation: AAC74014.1 .
    AP009048 Genomic DNA. Translation: BAA35674.1 .
    PIRi A00598. XNECD.
    RefSeqi NP_415448.1. NC_000913.3.
    YP_489200.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AAM X-ray 2.80 A 1-396 [» ]
    1AAW X-ray 2.40 A 1-396 [» ]
    1AHE X-ray 2.30 A/B 1-396 [» ]
    1AHF X-ray 2.30 A/B 1-396 [» ]
    1AHG X-ray 2.50 A/B 1-396 [» ]
    1AHX X-ray 2.00 A/B 1-396 [» ]
    1AHY X-ray 2.30 A/B 1-396 [» ]
    1AIA X-ray 2.20 A/B 1-396 [» ]
    1AIB X-ray 2.80 A/B 1-396 [» ]
    1AIC X-ray 2.40 A/B 1-396 [» ]
    1AMQ X-ray 2.20 A 1-396 [» ]
    1AMR X-ray 2.10 A 1-396 [» ]
    1AMS X-ray 2.70 A 1-396 [» ]
    1ARG X-ray 2.20 A/B 1-396 [» ]
    1ARH X-ray 2.30 A/B 1-396 [» ]
    1ARI X-ray 2.30 A/B 1-396 [» ]
    1ARS X-ray 1.80 A 1-396 [» ]
    1ART X-ray 1.80 A 1-396 [» ]
    1ASA X-ray 2.40 A 1-396 [» ]
    1ASB X-ray 2.60 A 1-396 [» ]
    1ASC X-ray 2.40 A 1-396 [» ]
    1ASD X-ray 2.20 A 1-396 [» ]
    1ASE X-ray 2.50 A 1-396 [» ]
    1ASF X-ray 2.80 A 1-396 [» ]
    1ASG X-ray 2.80 A 1-396 [» ]
    1ASL X-ray 2.60 A/B 1-396 [» ]
    1ASM X-ray 2.35 A/B 1-396 [» ]
    1ASN X-ray 2.50 A/B 1-396 [» ]
    1B4X X-ray 2.45 A 1-396 [» ]
    1BQA X-ray 2.10 A/B 1-396 [» ]
    1BQD X-ray 2.10 A/B 1-396 [» ]
    1C9C X-ray 2.40 A 1-396 [» ]
    1CQ6 X-ray 2.70 A 1-396 [» ]
    1CQ7 X-ray 2.40 A 1-396 [» ]
    1CQ8 X-ray 2.40 A 1-396 [» ]
    1CZC X-ray 2.50 A 1-396 [» ]
    1CZE X-ray 2.40 A 1-396 [» ]
    1G4V X-ray 2.00 A 1-396 [» ]
    1G4X X-ray 2.20 A 1-396 [» ]
    1G7W X-ray 2.20 A 1-396 [» ]
    1G7X X-ray 2.20 A 1-396 [» ]
    1IX6 X-ray 2.20 A 1-396 [» ]
    1IX7 X-ray 2.20 A 1-396 [» ]
    1IX8 X-ray 2.20 A 1-396 [» ]
    1QIR X-ray 2.20 A 1-396 [» ]
    1QIS X-ray 1.90 A 1-396 [» ]
    1QIT X-ray 1.90 A 1-396 [» ]
    1SPA X-ray 2.00 A 1-396 [» ]
    1TOE X-ray 2.00 A 1-388 [» ]
    1TOG X-ray 2.31 A/B 1-388 [» ]
    1TOI X-ray 1.90 A 1-388 [» ]
    1TOJ X-ray 1.90 A 1-388 [» ]
    1TOK X-ray 1.85 A/B 1-388 [» ]
    1X28 X-ray 2.40 A/B 1-396 [» ]
    1X29 X-ray 2.20 A/B 1-396 [» ]
    1X2A X-ray 2.20 A/B 1-396 [» ]
    1YOO X-ray 2.40 A 1-396 [» ]
    2AAT X-ray 2.80 A 1-396 [» ]
    2D5Y X-ray 1.98 A 1-396 [» ]
    2D61 X-ray 2.01 A 1-396 [» ]
    2D63 X-ray 2.05 A 1-396 [» ]
    2D64 X-ray 2.05 A 1-396 [» ]
    2D65 X-ray 2.30 A 1-396 [» ]
    2D66 X-ray 2.18 A 1-396 [» ]
    2D7Y X-ray 2.66 A 1-396 [» ]
    2D7Z X-ray 2.65 A 1-396 [» ]
    2Q7W X-ray 1.40 A 1-396 [» ]
    2QA3 X-ray 1.75 A 1-396 [» ]
    2QB2 X-ray 1.70 A 1-396 [» ]
    2QB3 X-ray 1.45 A 1-396 [» ]
    2QBT X-ray 1.75 A 1-396 [» ]
    3AAT X-ray 2.80 A 1-396 [» ]
    3QN6 X-ray 1.79 A 1-396 [» ]
    3QPG X-ray 1.79 A 1-396 [» ]
    3ZZJ X-ray 2.50 A 1-396 [» ]
    3ZZK X-ray 1.78 A 1-396 [» ]
    4A00 X-ray 2.34 A 1-396 [» ]
    4DBC X-ray 1.50 A 1-396 [» ]
    4F5F X-ray 2.25 A/B 2-396 [» ]
    4F5G X-ray 1.67 A/B 2-396 [» ]
    4F5H X-ray 1.60 A/B 2-396 [» ]
    4F5I X-ray 2.20 A/B 2-396 [» ]
    4F5J X-ray 1.95 A/B 2-396 [» ]
    4F5K X-ray 2.20 A/B 2-396 [» ]
    4F5L X-ray 1.40 A/B 2-396 [» ]
    4F5M X-ray 1.65 A/B 2-396 [» ]
    5EAA X-ray 2.40 A 1-396 [» ]
    ProteinModelPortali P00509.
    SMRi P00509. Positions 1-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9181N.
    IntActi P00509. 4 interactions.
    STRINGi 511145.b0928.

    2D gel databases

    SWISS-2DPAGE P00509.

    Proteomic databases

    PaxDbi P00509.
    PRIDEi P00509.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74014 ; AAC74014 ; b0928 .
    BAA35674 ; BAA35674 ; BAA35674 .
    GeneIDi 12931027.
    945553.
    KEGGi ecj:Y75_p0900.
    eco:b0928.
    PATRICi 32117069. VBIEscCol129921_0959.

    Organism-specific databases

    EchoBASEi EB0094.
    EcoGenei EG10096. aspC.

    Phylogenomic databases

    eggNOGi COG1448.
    HOGENOMi HOG000185899.
    KOi K00813.
    OMAi RVGACTI.
    OrthoDBi EOG6C2WBK.
    PhylomeDBi P00509.

    Enzyme and pathway databases

    BioCyci EcoCyc:ASPAMINOTRANS-MONOMER.
    ECOL316407:JW0911-MONOMER.
    MetaCyc:ASPAMINOTRANS-MONOMER.
    BRENDAi 2.6.1.1. 2026.
    SABIO-RK P00509.

    Miscellaneous databases

    EvolutionaryTracei P00509.
    PROi P00509.

    Gene expression databases

    Genevestigatori P00509.

    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 complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes."
      Kondo K., Wakabayashi S., Yagi T., Kagamiyama H.
      Biochem. Biophys. Res. Commun. 122:62-67(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene."
      Kuramitsu S., Okuno S., Ogawa T., Ogawa H., Kagamiyama H.
      J. Biochem. 97:1259-1262(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes."
      Fotheringham I.G., Dacey S.A., Taylor P.P., Smith T.J., Hunter M.G., Finlay M.E., Primrose S.B., Parker D.M., Edwards R.M.
      Biochem. J. 234:593-604(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure."
      Kondo K., Wakabayashi S., Kagamiyama H.
      J. Biol. Chem. 262:8648-8657(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    9. "Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes."
      Inoue K., Kuramitsu S., Okamoto A., Hirotsu K., Higuchi T., Kagamiyama H.
      Biochemistry 30:7796-7801(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-65.
    10. "The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase."
      Yano T., Kuramitsu S., Tanase S., Morino Y., Hiromi K., Kagamiyama H.
      J. Biol. Chem. 266:6079-6085(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-133.
    11. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    12. "The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction."
      Mahon M.M., Graber R., Christen P., Malthouse J.P.
      Biochim. Biophys. Acta 1434:191-201(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-280 AND ARG-374.
    13. "2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli."
      Smith D.L., Almo S.C., Toney M.D., Ringe D.
      Biochemistry 28:8161-8167(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246.
    14. "Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase."
      Danishefsky A.T., Onnufer J.J., Petsko G.A., Ringe D.
      Biochemistry 30:1980-1985(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), MUTAGENESIS OF ARG-374.
    15. "Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues."
      Oue S., Okamoto A., Yano T., Kagamiyama H.
      J. Biol. Chem. 274:2344-2349(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT.
    16. "Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase."
      Mizuguchi H., Hayashi H., Okada K., Miyahara I., Hirotsu K., Kagamiyama H.
      Biochemistry 40:353-360(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-183/PHE-214; ALA-183/LEU-280; ALA-183/LEU-374 AND ALA-183/LEU-280/LEU-374 IN COMPLEXES WITH PYRIDOXAL PHOSPHATE, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-246.
    17. "Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals 'a tale of two mechanisms'."
      Liu D., Pozharski E., Lepore B.W., Fu M., Silverman R.B., Petsko G.A., Ringe D.
      Biochemistry 46:10517-10527(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND SADTA, PYRIDOXAL PHOSPHATE AT LYS-246.

    Entry informationi

    Entry nameiAAT_ECOLI
    AccessioniPrimary (citable) accession number: P00509
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3