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    argJ bifunctional ornithine acetyltransferase/N-acetylglutamate synthase [ Streptococcus mutans UA159 ]

    Gene ID: 1028088, updated on 30-Jan-2018

    Summary

    Gene symbol
    argJ
    Gene description
    bifunctional ornithine acetyltransferase/N-acetylglutamate synthase
    Locus tag
    SMU_664
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Streptococcus mutans UA159 (strain: UA159)
    Lineage
    Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus
    Old locus tag
    SMU.664

    Genomic context

    Sequence:
    NC_004350.2 (623123..624316)

    NC_004350.2Genomic Context describing neighboring genes Neighboring gene hypothetical protein Neighboring gene N-acetyl-gamma-glutamyl-phosphate reductase Neighboring gene acetylglutamate kinase Neighboring gene acetylornithine aminotransferase

    Pathways from BioSystems

    General protein information

    Names
    bifunctional ornithine acetyltransferase/N-acetylglutamate synthase
    NP_721092.1
    • Best Blastp Hit: dbj|BAB06618.1| (AP001517) ornithine acetyltransferase/amino-acid acetyltransferase [Bacillus halodurans]

    NCBI Reference Sequences (RefSeq)

    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_004350.2 Reference assembly

      Range
      623123..624316
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_721092.1 bifunctional ornithine acetyltransferase/N-acetylglutamate synthase [Streptococcus mutans UA159]

      See identical proteins and their annotated locations for NP_721092.1

      Status: PROVISIONAL

      UniProtKB/Swiss-Prot
      Q8DV45
      Conserved Domains (1) summary
      cd02152
      Location:11397
      OAT; Ornithine acetyltransferase (OAT) family; also referred to as ArgJ. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in ...
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