U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    torA trimethylamine N-oxide reductase 1 [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946267, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    torA
    Official Full Name
    trimethylamine N-oxide reductase 1
    Primary source
    ECOCYC:EG11814
    Locus tag
    b0997
    See related
    ASAP:ABE-0003372
    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
    ECK0988
    Summary
    Verified Tat substrate: [More information is available at EcoGene: EG11814]. TorA contains the active site and molybdenum cofactor . [More information is available at EcoCyc: EG11814].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (1059256..1061802)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene periplasmic trimethylamine-N-oxide binding protein Neighboring gene DNA-binding transcriptional dual regulator TorR Neighboring gene cytochrome c menaquinol dehydrogenase TorC Neighboring gene trimethylamine-N-oxide reductase-specific chaperone Neighboring gene chaperone modulator CbpM Neighboring gene curved DNA-binding protein

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway. Dow JM, et al. Biochem J, 2013 May 15. PMID 23452237, Free PMC Article
    2. Molybdenum cofactor: a compound in the in vitro activation of both nitrate reductase and trimethylamine-N-oxide reductase activities in Escherichia coli K12. Silvestro A, et al. Biochim Biophys Acta, 1986 Aug 15. PMID 3524687
    3. [Assessment of the Escherichia coli Tat protein translocation system with fluorescent proteins]. Zhang M, et al. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai), 2003 Aug. PMID 12897964
    4. Regulation of the trimethylamine N-oxide (TMAO) reductase in Escherichia coli: analysis of tor::Mud1 operon fusion. Pascal MC, et al. Mol Gen Genet, 1984. PMID 6387391
    5. Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli. Buc J, et al. Mol Microbiol, 1999 Apr. PMID 10216869

    See all (68) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
      Title: Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
    2. Immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Lon interacts with apoTorA but not with holoTorA.
      Title: Quality control of a molybdoenzyme by the Lon protease.
    3. 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.
    4. Translocation of TorA is directed by the TorD protein, which is a cytoplasmic chaperone known to interact physically with the TorA signal peptide.
      Title: Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway.
    5. N-terminus verified by Edman degradation on mature peptide
      Title: A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12.
    Submit: New GeneRIF Correction

    Pathways from PubChem

    Go to the top of the page

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables electron transfer activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables electron transfer activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables molybdenum ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables molybdenum ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables molybdopterin cofactor binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables molybdopterin cofactor binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables molybdopterin cofactor binding ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables trimethylamine-N-oxide reductase (cytochrome c) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables trimethylamine-N-oxide reductase (cytochrome c) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables trimethylamine-N-oxide reductase (cytochrome c) activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in aerobic respiration IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within aerobic respiration IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within anaerobic electron transport chain IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in anaerobic electron transport chain IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in anaerobic respiration IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within anaerobic respiration IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in regulation of pH IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in outer membrane-bounded periplasmic space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of trimethylamine-N-oxide reductase (cytochrome c) complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    trimethylamine N-oxide reductase 1

    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_000913.3 Reference assembly

      Range
      1059256..1061802
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415517.1 trimethylamine N-oxide reductase 1 [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415517.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A895NXR9
      Conserved Domains (1) summary
      PRK15102
      Location:10 → 836
      PRK15102; trimethylamine-N-oxide reductase TorA
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

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