U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    yyaE putative oxidoreductase (molybdoenzyme) [ Bacillus subtilis subsp. subtilis str. 168 ]

    Gene ID: 937914, updated on 6-Oct-2023

    Summary

    Go to the top of the page Help
    Gene symbol
    yyaE
    Gene description
    putative oxidoreductase (molybdoenzyme)
    Locus tag
    BSU_40930
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Bacillus subtilis subsp. subtilis str. 168 (strain: 168, sub-species: subtilis, type-material: type strain of Bacillus subtilis)
    Lineage
    Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus
    Old locus tag
    BSU40930
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000964.3 (4201070..4203073, complement)

    NC_000964.3Genomic Context describing neighboring genes Neighboring gene ribosomal protein S6 (BS9) Neighboring gene potassium-dependent informational ATPase interacting with 70S ribosome; ROS stress regulator Neighboring gene putative nucleic acid binding protein Neighboring gene putative transporter

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000964.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement. Borriss R, et al. Microb Biotechnol, 2018 Jan. PMID 29280348, Free PMC Article
    2. An updated metabolic view of the Bacillus subtilis 168 genome. Belda E, et al. Microbiology (Reading), 2013 Apr. PMID 23429746
    3. From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later. Barbe V, et al. Microbiology (Reading), 2009 Jun. PMID 19383706, Free PMC Article
    4. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Kunst F, et al. Nature, 1997 Nov 20. PMID 9384377

    GeneRIFs: Gene References Into Functions

    General gene information

    Go to the top of the page Help

    Homology

    General protein information

    Go to the top of the page Help
    Preferred Names
    putative oxidoreductase (molybdoenzyme)
    NP_391973.1
    • Evidence 3: Putative function from multiple computational evidences; PubMedId: 17114254, 20817769; Product type e: enzyme

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000964.3 Reference assembly

      Range
      4201070..4203073 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_391973.1 putative oxidoreductase (molybdoenzyme) [Bacillus subtilis subsp. subtilis str. 168]

      See identical proteins and their annotated locations for NP_391973.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A0D1KMU9
      Conserved Domains (2) summary
      cd02766
      Location:7 → 534
      MopB_3; The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members ...
      cl09929
      Location:554 → 667
      MopB_CT; Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P37519.1

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Other Literature Sources
    Molecular Biology Databases