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    aspC aspartate aminotransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945553, updated on 4-Apr-2024

    Summary

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    Gene symbol
    aspC
    Gene description
    aspartate aminotransferase
    Primary source
    ASAP:ABE-0003150
    Locus tag
    b0928
    See related
    ECOCYC:EG10096
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK0919
    Summary
    Aspartate aminotransferase (AspC) is a multifunctional enzyme that catalyzes the synthesis of aspartate, phenylalanine and other compounds via a transamination reaction. [More information is available at EcoCyc: EG10096].
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    Genomic context

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    Sequence:
    NC_000913.3 (984519..985709, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene peptidoglycan L,D-endopeptidase Neighboring gene hydroxyacylglutathione hydrolase GloC Neighboring gene outer membrane porin F Neighboring gene asparagine--tRNA ligase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structure. Deu E, et al. Biochemistry, 2009 Jan 20. PMID 19099423
    2. Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme. Deu E, et al. Biochemistry, 2007 May 15. PMID 17441730
    3. The unfolding pathway for Apo Escherichia coli aspartate aminotransferase is dependent on the choice of denaturant. Deu E, et al. Biochemistry, 2007 May 15. PMID 17425331
    4. Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase. Chow MA, et al. Biochemistry, 2004 Oct 12. PMID 15461450
    5. Reaction of aspartate aminotransferase with C5-dicarboxylic acids: comparison with the reaction with C4-dicarboxylic acids. Islam MM, et al. J Biochem, 2003 Aug. PMID 12966078

    See all (101) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Deletion of aspartate aminotransferase and sfcA (both involved in oxaloacetate metabolism), together with deletions of other ferementation disruption genes significantly increased succinate yield
      Title: Eliminating side products and increasing succinate yields in engineered strains of Escherichia coli C.
    2. N-terminus verified by Edman degradation on complete protein
      Title: Kynurenine aminotransferase and glutamine transaminase K of Escherichia coli: identity with aspartate aminotransferase.
    3. Pyridoxal phosphate, which binds at intersubunit active sites, stabilizes native form by 6 kcal mol-1 & dissociates during the D <==> D* transition. Reductive trapping of cofactor to nondissociable derivative (PPL-eAATase) precludes the formation of D*.
      Title: Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme.
    4. urea-mediated denaturation of eAATase finds no evidence for an M* species but uncovers a partially denatured dimeric form, D*, that is unpopulated in GdnHCl. unfolding process is a function of the employed denaturant.
      Title: The unfolding pathway for Apo Escherichia coli aspartate aminotransferase is dependent on the choice of denaturant.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables L-aspartate:2-oxoglutarate aminotransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables L-aspartate:2-oxoglutarate aminotransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables L-aspartate:2-oxoglutarate aminotransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables L-tyrosine:2-oxoglutarate aminotransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables L-tyrosine:2-oxoglutarate aminotransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables pyridoxal phosphate binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables pyridoxal phosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables pyridoxal phosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transaminase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within L-phenylalanine biosynthetic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in L-phenylalanine biosynthetic process from chorismate via phenylpyruvate IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within L-phenylalanine biosynthetic process from chorismate via phenylpyruvate IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in amino acid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    aspartate aminotransferase
    NP_415448.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      984519..985709 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415448.1 aspartate aminotransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415448.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A485JK82, Q304P7
      Conserved Domains (1) summary
      PRK09257
      Location:1 → 396
      PRK09257; aromatic amino acid transaminase
    Nucleotide Protein
    Heading Accession and Version

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