U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    sdhB succinate:quinone oxidoreductase, iron-sulfur cluster binding protein [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945300, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    sdhB
    Official Full Name
    succinate:quinone oxidoreductase, iron-sulfur cluster binding protein
    Primary source
    ECOCYC:EG10932
    Locus tag
    b0724
    See related
    ASAP:ABE-0002468
    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
    dhsB; ECK0713
    Summary
    The sdhABCD operon is negatively regulated by ryhB RNA as part of indirect positive regulation by Fur. [More information is available at EcoGene: EG10932]. This is one of two catalytic subunits of the four subunit enzyme. [More information is available at EcoCyc: EG10932].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (757689..758405)

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

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Out of plane distortions of the heme b of Escherichia coli succinate dehydrogenase. Tran QM, et al. PLoS One, 2012. PMID 22393428, Free PMC Article
    2. Fumarate-Mediated Persistence of Escherichia coli against Antibiotics. Kim JS, et al. Antimicrob Agents Chemother, 2016 Apr. PMID 26810657, Free PMC Article
    3. The quinone-binding and catalytic site of complex II. Maklashina E, et al. Biochim Biophys Acta, 2010 Dec. PMID 20175986, Free PMC Article
    4. Evidence for non-cysteinyl coordination of the [2Fe-2S] cluster in Escherichia coli succinate dehydrogenase. Werth MT, et al. FEBS Lett, 1992 Mar 24. PMID 1312028
    5. Evidence that centre 2 in Escherichia coli fumarate reductase is a [4Fe-4S]cluster. Cammack R, et al. Biochim Biophys Acta, 1986 Apr 22. PMID 3008846

    See all (82) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. SDH and FRD represent a paired system that gives rise to and maintains E. coli antibiotic-resistant persisters by producing and utilizing fumarate, respectively.
      Title: Fumarate-Mediated Persistence of Escherichia coli against Antibiotics.
    2. We demonstrate that the FAD assembly factor SdhE, which flavinylates and activates the respiratory enzyme succinate dehydrogenase (SDH), is also required for the complete activation and flavinylation of fumarate reductase .
      Title: The succinate dehydrogenase assembly factor, SdhE, is required for the flavinylation and activation of fumarate reductase in bacteria.
    3. Out of plane distortions of the heme b of Escherichia coli succinate dehydrogenase
      Title: Out of plane distortions of the heme b of Escherichia coli succinate dehydrogenase.
    4. 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.
    5. N-terminus verified by Edman degradation on complete protein
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    6. iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow
      Title: The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow.
    Submit: New GeneRIF Correction

    Pathways from PubChem

    Go to the top of the page

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables 2 iron, 2 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 2 iron, 2 sulfur cluster binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables 3 iron, 4 sulfur cluster binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 3 iron, 4 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 4 iron, 4 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 4 iron, 4 sulfur cluster binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables electron transfer activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables electron transfer activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables iron-sulfur cluster binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables iron-sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity 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
    		  
    Process Evidence Code Pubs
    involved_in aerobic electron transport chain NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in aerobic respiration IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within aerobic respiration IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in respiratory electron transport chain IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tricarboxylic acid cycle IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in membrane NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    succinate:quinone oxidoreductase, iron-sulfur cluster binding protein
    NP_415252.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      757689..758405
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415252.1 succinate:quinone oxidoreductase, iron-sulfur cluster binding protein [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415252.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9AAB3, A0A8S7EJ05
      Conserved Domains (1) summary
      PRK05950
      Location:4 → 236
      sdhB; succinate dehydrogenase iron-sulfur subunit; Reviewed
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.