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    ispU ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944874, updated on 17-Dec-2024

    Summary

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    Official Symbol
    ispU
    Official Full Name
    ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
    Primary source
    ECOCYC:G6092
    Locus tag
    b0174
    See related
    ASAP:ABE-0000595
    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
    ECK0173; rth; uppS; yaeS
    Summary
    Undecaprenyl diphosphate (UPP) synthase catalyzes the condensation reactions resulting in the formation of UPP, a di-trans,poly-cis-undecaprenyl pyrophosphate that functions as the lipid carrier for bacterial cell wall carbohydrates. [More information is available at EcoCyc: G6092].
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    Genomic context

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    Sequence:
    NC_000913.3 (194903..195664)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 1-deoxy-D-xylulose 5-phosphate reductoisomerase Neighboring gene ncRNA Neighboring gene CDP-diglyceride synthetase Neighboring gene intramembrane zinc metalloprotease RseP

    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. Mechanism of cis-prenyltransferase reaction probed by substrate analogues. Lu YP, et al. Biochem Biophys Res Commun, 2010 Oct 1. PMID 20828539
    2. Photoaffinity labeling of undecaprenyl pyrophosphate synthetase with a farnesyl pyrophosphate analogue. Baba T, et al. J Biol Chem, 1985 Sep 5. PMID 3897217
    3. Molecular analysis of prenyl chain elongating enzymes. Koyama T. Biosci Biotechnol Biochem, 1999 Oct. PMID 10586494
    4. Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. Pan JJ, et al. Biochemistry, 2000 Sep 5. PMID 10978182
    5. Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis. Pan JJ, et al. Biochemistry, 2000 Nov 14. PMID 11076526

    See all (26) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Here, we report that a mutation altering the UppS enzyme that synthesizes undecaprenyl phosphate prevents cells from growing at high temperatures, and that compensatory mutations in enzymes functioning upstream of UppS can reverse this phenotype
      Title: A Defective Undecaprenyl Pyrophosphate Synthase Induces Growth and Morphological Defects That Are Suppressed by Mutations in the Isoprenoid Pathway of Escherichia coli.
    2. Unlike the sequential mechanism used by trans-prenyltransferases, these data demonstrate E. coli UPPS utilizes the concerted mechanism.
      Title: Mechanism of cis-prenyltransferase reaction probed by substrate analogues.
    3. N-terminus verified by Edman degradation on complete protein
      Title: Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene.
    4. L85, L88 or F89 are important for substrate binding but not specificity. The upper portion of the active-site tunnel, where cis double bonds of the product reside, may be critical for determining the final product chain length.
      Title: Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase.
    5. undecaprenyl pyrophosphate synthase (UPPs)is crystallized in a new trigonal unit cell with Mg(2+)/isopentenyl pyrophosphates (IPP)/farnesyl thiopyrophosphate bound to the active site
      Title: Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    contributes_to dehydrodolichyl diphosphate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables di-trans,poly-cis-undecaprenyl-diphosphate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables di-trans,poly-cis-undecaprenyl-diphosphate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables di-trans,poly-cis-undecaprenyl-diphosphate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables small molecule binding EXP
    Inferred from Experiment
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity, transferring alkyl or aryl (other than methyl) groups IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within Gram-negative-bacterium-type cell wall biogenesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cell division IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cell wall organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in peptidoglycan biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within peptidoglycan biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in polyprenol biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within polyprenol biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of cell shape IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
    NP_414716.1

    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
      194903..195664
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414716.1 ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414716.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0AAJ3P328, A0AAN1S2F0, A0AAP8AX79
      Conserved Domains (1) summary
      PRK10240
      Location:25 → 253
      PRK10240; (2E,6E)-farnesyl-diphosphate-specific ditrans,polycis-undecaprenyl-diphosphate synthase
    Nucleotide Protein
    Heading Accession and Version

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