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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
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