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    sucA subunit of E1(0) component of 2-oxoglutarate dehydrogenase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945303, updated on 3-Dec-2024

    Summary

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    Official Symbol
    sucA
    Official Full Name
    subunit of E1(0) component of 2-oxoglutarate dehydrogenase
    Primary source
    ECOCYC:EG10979
    Locus tag
    b0726
    See related
    ASAP:ABE-0002478
    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
    ECK0714; lys+met
    Summary
    sucAB is a synthetic lethal with sucCD. [More information is available at EcoGene: EG10979]. SucA is the E1(0) component of the oxoglutarate dehydrogenase complex. [More information is available at EcoCyc: EG10979].
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    Genomic context

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    Sequence:
    NC_000913.3 (758706..761507)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene succinate:quinone oxidoreductase, membrane protein SdhD Neighboring gene succinate:quinone oxidoreductase, FAD binding protein Neighboring gene succinate:quinone oxidoreductase, iron-sulfur cluster binding protein Neighboring gene dihydrolipoyltranssuccinylase Neighboring gene succinyl-CoA synthetase subunit beta Neighboring gene succinyl-CoA synthetase subunit alpha

    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. Alpha-keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex. Pettit FH, et al. J Biol Chem, 1973 Aug 10. PMID 4588679
    2. Off-pathway, oxygen-dependent thiamine radical in the Krebs cycle. Frank RA, et al. J Am Chem Soc, 2008 Feb 6. PMID 18183975, Free PMC Article
    3. 2-Oxo acid dehydrogenase multienzyme complexes: domains, dynamics, and design. Perham RN, et al. Ann N Y Acad Sci, 1989. PMID 2699393
    4. Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. Frank RA, et al. J Mol Biol, 2007 May 4. PMID 17367808, Free PMC Article
    5. Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12. Darlison MG, et al. Eur J Biochem, 1984 Jun 1. PMID 6376123

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxoglutarate dehydrogenase (succinyl-transferring) activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables oxoglutarate dehydrogenase (succinyl-transferring) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables oxoglutarate dehydrogenase (succinyl-transferring) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables thiamine pyrophosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables thiamine pyrophosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in tricarboxylic acid cycle IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tricarboxylic acid cycle IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in tricarboxylic acid cycle IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of oxoglutarate dehydrogenase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of oxoglutarate dehydrogenase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    subunit of E1(0) component of 2-oxoglutarate dehydrogenase
    NP_415254.1

    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
      758706..761507
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415254.1 subunit of E1(0) component of 2-oxoglutarate dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415254.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2H4TNT3, A0A376DDS9, A0A828PKS4, A0A8S7XUH2, A0A8T3UK27, A0AAN5UHF7
      Conserved Domains (1) summary
      PRK09404
      Location:2 → 931
      sucA; 2-oxoglutarate dehydrogenase E1 component; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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