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    mobA molybdenum cofactor guanylyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948349, updated on 17-Dec-2024

    Summary

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    Official Symbol
    mobA
    Official Full Name
    molybdenum cofactor guanylyltransferase
    Primary source
    ECOCYC:EG11829
    Locus tag
    b3857
    See related
    ASAP:ABE-0012593
    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
    chlB; ECK3849; mob; narB
    Summary
    In all enzymes that utilize molybdenum and tungsten cofactors (with the exception of nitrogenase) the metals 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: EG11829].
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    Genomic context

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    Sequence:
    NC_000913.3 (4041415..4041999, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 23S ribosomal RNA Neighboring gene 5S ribosomal RNA Neighboring gene molybdopterin-guanine dinucleotide biosynthesis adaptor protein Neighboring gene DUF1040 domain-containing protein YihD Neighboring gene stress response kinase A

    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. The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters. Rothery RA, et al. J Biol Chem, 1998 Mar 27. PMID 9516445
    2. Mapping of the gene chl-B controlling membran bound nitrate reductase and formic hydrogen-lyase activities in Escherichia coli K 12. Casse F. Biochem Biophys Res Commun, 1970 May 11. PMID 4912199
    3. Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli. Palmer T, et al. Eur J Biochem, 1994 Jun 1. PMID 8020507
    4. Involvement of a low-molecular-weight substance in in vitro activation of the molybdoenzyme respiratory nitrate reductase from a chlB mutant of Escherichia coli. Boxer DH, et al. J Bacteriol, 1987 Oct. PMID 3308848, Free PMC Article
    5. The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis. Lake MW, et al. J Biol Chem, 2000 Dec 22. PMID 10978347

    See all (28) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data indicate that bis-MGD formed by MobA is fully functional and restores the catalytic activity in apoTorA.
      Title: Identification of a bis-molybdopterin intermediate in molybdenum cofactor biosynthesis in Escherichia coli.
    2. N-terminus verified by Edman degradation on complete protein
      Title: Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli.
    Submit: New GeneRIF Correction

    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 GTP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables guanylyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables molybdenum cofactor guanylyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables molybdenum cofactor guanylyltransferase 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 transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in Mo-molybdopterin cofactor biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in Mo-molybdopterin cofactor metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    molybdenum cofactor guanylyltransferase
    NP_418294.1

    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
      4041415..4041999 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418294.1 molybdenum cofactor guanylyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418294.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0AAN3M7R8
      Conserved Domains (1) summary
      PRK00317
      Location:4 → 194
      mobA; molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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