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    gpmM 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948130, updated on 17-Dec-2024

    Summary

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    Official Symbol
    gpmM
    Official Full Name
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase
    Primary source
    ECOCYC:EG12296
    Locus tag
    b3612
    See related
    ASAP:ABE-0011818
    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
    ECK3602; gpmC; gpmI; pgmI; yibO
    Summary
    Characterization of the Salmonella GpmM: [More information is available at EcoGene: EG12296].
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    Genomic context

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    Sequence:
    NC_000913.3 (3785260..3786804)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene reduced glutaredoxin 3 Neighboring gene putative sulfurtransferase YibN Neighboring gene murein hydrolase activator EnvC Neighboring gene divergent polysaccharide deacetylase domain-containing protein YibQ Neighboring gene UDP-glucuronate:LPS(HepIII) glycosyltransferase

    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. Comparison of the binuclear metalloenzymes diphosphoglycerate-independent phosphoglycerate mutase and alkaline phosphatase: their mechanism of catalysis via a phosphoserine intermediate. Jedrzejas MJ, et al. Chem Rev, 2001 Mar. PMID 11712498
    2. Glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, and phosphoglyceromutase of Escherichia coli. Simultaneous purification and physical properties. D'Alessio G, et al. J Biol Chem, 1971 Jul 10. PMID 4932978
    3. Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria. Kehres DG, et al. FEMS Microbiol Rev, 2003 Jun. PMID 12829271
    4. Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase. Jedrzejas MJ. Prog Biophys Mol Biol, 2000. PMID 10958932
    5. The two analogous phosphoglycerate mutases of Escherichia coli. Fraser HI, et al. FEBS Lett, 1999 Jul 23. PMID 10437801

    See all (16) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    General gene information

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    Homology

    General protein information

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    Preferred Names
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase
    NP_418069.1

    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
      3785260..3786804
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418069.1 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418069.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376M0K5
      Conserved Domains (1) summary
      PRK05434
      Location:4 → 512
      PRK05434; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
    Nucleotide Protein
    Heading Accession and Version

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