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    ispD 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948269, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ispD
    Official Full Name
    2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
    Primary source
    ECOCYC:G7423
    Locus tag
    b2747
    See related
    ASAP:ABE-0009017
    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
    ECK2742; ygbP
    Summary
    IspD is also called 4-diphosphocytidyl-2-C-methylerythritol synthase. [More information is available at EcoGene: EG13110]. 4-diphosphocytidyl-2C-methyl-D-erythritol synthase (IspD) catalyzes the third step in the methylerythritol phosphate pathway. [More information is available at EcoCyc: G7423].
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    Genomic context

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    Sequence:
    NC_000913.3 (2871780..2872490, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene protein-L-isoaspartate O-methyltransferase Neighboring gene broad specificity 5'(3')-nucleotidase and polyphosphatase Neighboring gene tRNA pseudouridine(13) synthase Neighboring gene 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Neighboring gene cell division protein FtsB Neighboring gene DUF3561 domain-containing inner membrane protein YgbE

    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. Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis. Richard SB, et al. Nat Struct Biol, 2001 Jul. PMID 11427897
    2. Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and mutants, reveals roles of active site amino acids. Richard SB, et al. Biochemistry, 2004 Sep 28. PMID 15379557
    3. Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. Kemp LE, et al. Acta Crystallogr D Biol Crystallogr, 2003 Mar. PMID 12595740
    4. Crystallization and preliminary X-ray diffraction studies of recombinant Escherichia coli 4-diphosphocytidyl-2-C-methyl-D-erythritol synthetase. Kemp LE, et al. Acta Crystallogr D Biol Crystallogr, 2001 Aug. PMID 11468415
    5. The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate. Gabrielsen M, et al. FEBS J, 2006 Mar. PMID 16478479

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on mature peptide
      Title: Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol.
    2. quaternary structure and feedback regulation of enzyme activity
      Title: The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate.
    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 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables nucleotidyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in isoprenoid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
    NP_417227.1

    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
      2871780..2872490 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417227.1 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417227.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376FVQ6, A0A376M5T8
      Conserved Domains (1) summary
      PRK00155
      Location:8 → 232
      ispD; D-ribitol-5-phosphate cytidylyltransferase
    Nucleotide Protein
    Heading Accession and Version

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