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    sdhA succinate:quinone oxidoreductase, FAD binding protein [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945402, updated on 17-Dec-2024

    Summary

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    Official Symbol
    sdhA
    Official Full Name
    succinate:quinone oxidoreductase, FAD binding protein
    Primary source
    ECOCYC:EG10931
    Locus tag
    b0723
    See related
    ASAP:ABE-0002466
    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
    dhsA; ECK0712
    Summary
    The sdhABCD operon is negatively regulated by ryhB RNA as part of indirect positive regulation by Fur. [More information is available at EcoGene: EG10931]. This is one of two catalytic subunits in the four subunit enzyme. [More information is available at EcoCyc: EG10931].
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    Genomic context

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    Sequence:
    NC_000913.3 (755907..757673)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene protein YbgV Neighboring gene protein YbgU Neighboring gene succinate:quinone oxidoreductase, membrane protein SdhC Neighboring gene succinate:quinone oxidoreductase, membrane protein SdhD Neighboring gene succinate:quinone oxidoreductase, iron-sulfur cluster binding protein Neighboring gene subunit of E1(0) component of 2-oxoglutarate dehydrogenase

    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. [Integration and expression of sdh gene in Escherichia coli]. Gao SY, et al. Wei Sheng Wu Xue Bao, 2005 Feb. PMID 15847182
    2. The quinone-binding and catalytic site of complex II. Maklashina E, et al. Biochim Biophys Acta, 2010 Dec. PMID 20175986, Free PMC Article
    3. Suppression of the succinate requirement of lipoamide dehydrogenase mutants of Escherichia coli by mutations affecting succinate dehydrogenase activity. Creaghan IT, et al. J Gen Microbiol, 1977 Sep. PMID 335020
    4. Studies on succinate dehydrogenase. XX. Amino acid sequence around the flavin site. Kenney WC, et al. J Biol Chem, 1972 Jul 25. PMID 4339718
    5. Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Mattevi A, et al. Structure, 1999 Jul 15. PMID 10425677

    See all (81) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data suggest thatthe quinone within the quinone-binding pocket of comolex II is essential for catalysis.
      Title: The quinone-binding and catalytic site of complex II.
    2. N-terminus verified by Edman degradation on complete protein
      Title: '98 Escherichia coli SWISS-2DPAGE database update.
    3. structural and catalytic analyses of the FrdA E49Q and SdhA Q50E mutants suggest that coulombic effects and the electronic state of the FAD are critical for directionality of the succinate/fumarate interconversions
      Title: Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain.
    Submit: New GeneRIF Correction

    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 electron transfer activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables electron transfer activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables electron transfer activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables flavin adenine dinucleotide binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables flavin adenine dinucleotide binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables flavin adenine dinucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity, acting on the CH-CH group of donors IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables succinate dehydrogenase (quinone) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables succinate dehydrogenase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables succinate dehydrogenase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in aerobic electron transport chain NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within aerobic respiration IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within aerobic respiration IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in anaerobic respiration IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in electron transport chain IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tricarboxylic acid cycle IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tricarboxylic acid cycle IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within tricarboxylic acid cycle IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in membrane NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of respiratory chain complex II (succinate dehydrogenase) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of respiratory chain complex II (succinate dehydrogenase) IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    succinate:quinone oxidoreductase, FAD binding protein
    NP_415251.1

    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
      755907..757673
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415251.1 succinate:quinone oxidoreductase, FAD binding protein [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415251.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A0H2YWW0, A0A192CK33, A0A1X3JKA6, A0AA36KVE5, F4SW44, Q1REK2
      Conserved Domains (1) summary
      PRK08958
      Location:1 → 588
      sdhA; succinate dehydrogenase flavoprotein subunit; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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