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    moeB molybdopterin-synthase adenylyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945452, updated on 17-Dec-2024

    Summary

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    Official Symbol
    moeB
    Official Full Name
    molybdopterin-synthase adenylyltransferase
    Primary source
    ECOCYC:EG10154
    Locus tag
    b0826
    See related
    ASAP:ABE-0002820
    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
    chlN; ECK0816
    Summary
    Molybdenum and tungsten cofactors of all enzymes, with the exception of nitrogenase, that require one or the other of the other for activity are present in an oxidized state as molybdate or tungstate ions that are chelated by the cis-dithiolene moiety of a molybdenum cofactor. [More information is available at EcoCyc: EG10154].
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    Genomic context

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    Sequence:
    NC_000913.3 (864380..865129, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative pyruvate formate-lyase activating enzyme YbiY Neighboring gene fructose-6-phosphate aldolase 1 Neighboring gene molybdopterin molybdotransferase Neighboring gene isoaspartyl dipeptidase proenzyme Neighboring gene glutathione ABC transporter ATP binding subunit GsiA

    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. Reconstitution of plant nitrate reductase by Escherichia coli extracts and the molecular cloning of the chlA gene of Escherichia coli K12. Taylor JL, et al. J Mol Appl Genet, 1983. PMID 6363588
    2. Nitrate reductase activity and heterocyst suppression on nitrate in Anabaena sp. strain PCC 7120 require moeA. Ramaswamy KS, et al. J Bacteriol, 1996 Jul. PMID 8682795, Free PMC Article
    3. Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Schmitz J, et al. Biochemistry, 2007 Jan 23. PMID 17223713
    4. Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis. Nohno T, et al. J Bacteriol, 1988 Sep. PMID 3045084, Free PMC Article
    5. IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli. Zhang W, et al. J Biol Chem, 2010 Jan 22. PMID 19946146, Free PMC Article

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    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 metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables molybdopterin-synthase adenylyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables molybdopterin-synthase adenylyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotidyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables nucleotidyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables sulfotransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables thiosulfate sulfurtransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ubiquitin-like modifier activating enzyme activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in Mo-molybdopterin cofactor biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in Mo-molybdopterin cofactor biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within Mo-molybdopterin cofactor biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    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 molybdopterin adenylyltransferase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    molybdopterin-synthase adenylyltransferase
    NP_415347.1

    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
      864380..865129 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415347.1 molybdopterin-synthase adenylyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415347.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8H9XMY2, A0A8S7EBK3
      Conserved Domains (1) summary
      PRK05690
      Location:1 → 244
      PRK05690; molybdopterin biosynthesis protein MoeB; Provisional
    Nucleotide Protein
    Heading Accession and Version

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