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    sucC succinyl-CoA synthetase subunit beta [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945312, updated on 3-Dec-2024

    Summary

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    Official Symbol
    sucC
    Official Full Name
    succinyl-CoA synthetase subunit beta
    Primary source
    ECOCYC:EG10981
    Locus tag
    b0728
    See related
    ASAP:ABE-0002483
    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
    ECK0716
    Summary
    sucCD is a synthetic lethal with sucAB. [More information is available at EcoGene: EG10981]. ACTIVE.SITES: [More information is available at EcoCyc: EG10981].
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    Genomic context

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    Sequence:
    NC_000913.3 (763014..764180)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene subunit of E1(0) component of 2-oxoglutarate dehydrogenase Neighboring gene dihydrolipoyltranssuccinylase Neighboring gene succinyl-CoA synthetase subunit alpha Neighboring gene ncRNA

    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. Novel mechanisms of Escherichia coli succinyl-coenzyme A synthetase regulation. Birney M, et al. J Bacteriol, 1996 May. PMID 8631677, Free PMC Article
    2. ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography. Joyce MA, et al. Biochemistry, 2000 Jan 11. PMID 10625475
    3. Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. Histidine 142 alpha is a facilitative catalytic residue. Luo GX, et al. J Biol Chem, 1991 Nov 5. PMID 1939128
    4. The subunits of succinyl-coenzyme A synthetase--function and assembly. Bridger WA, et al. Biochem Soc Symp, 1987. PMID 3332988
    5. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. Wolodko WT, et al. J Biol Chem, 1994 Apr 8. PMID 8144675

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. sucAB and sucCD are mutually essential genes for production of succinyl Coa that is essential for cell viability
      Title: sucAB and sucCD are mutually essential genes in Escherichia coli.
    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 ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables succinate-CoA ligase (ADP-forming) activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables succinate-CoA ligase (ADP-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables succinate-CoA ligase (ADP-forming) activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables succinate-CoA ligase (GDP-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in succinyl-CoA metabolic process IBA
    Inferred from Biological aspect of Ancestor
    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 IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tricarboxylic acid cycle NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 succinate-CoA ligase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of succinate-CoA ligase complex (ADP-forming) IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of succinate-CoA ligase complex (ADP-forming) IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    succinyl-CoA synthetase subunit beta
    NP_415256.1

    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
      763014..764180
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415256.1 succinyl-CoA synthetase subunit beta [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415256.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2X1PL10, A0A5N3D322, A0A775WV98
      Conserved Domains (1) summary
      PRK00696
      Location:1 → 388
      sucC; ADP-forming succinate--CoA ligase subunit beta
    Nucleotide Protein
    Heading Accession and Version

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