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    ssuE NADPH-dependent FMN reductase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945947, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ssuE
    Official Full Name
    NADPH-dependent FMN reductase
    Primary source
    ECOCYC:G6479
    Locus tag
    b0937
    See related
    ASAP:ABE-0003182
    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
    ECK0928; ssi4; ycbP
    Summary
    SsuD and SsuE form a stable complexand comprise a two-component alkanesulfonate monooxygenase system (Abdurachim, 2006). [More information is available at EcoGene: EG13708]. The SsuE protein is a NAD(P)H-dependent FMN reductase that provides FMNH2 for SsuD, an FMNH2-dependent monooxygenase . [More information is available at EcoCyc: G6479].
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    Genomic context

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    Sequence:
    NC_000913.3 (996937..997512, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene aliphatic sulfonate ABC transporter ATP binding subunit Neighboring gene aliphatic sulfonate ABC transporter membrane subunit Neighboring gene FMNH2-dependent alkanesulfonate monooxygenase Neighboring gene aliphatic sulfonate ABC transporter periplasmic binding protein Neighboring gene putative laminin-binding fimbrial subunit Neighboring gene putative fimbrial chaperone ElfD

    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. Crystal structure of Escherichia coli SsuE: defining a general catalytic cycle for FMN reductases of the flavodoxin-like superfamily. Driggers CM, et al. Biochemistry, 2014 Jun 3. PMID 24816272
    2. Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli. Gao B, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005 Sep 1. PMID 16511173, Free PMC Article
    3. Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli. Abdurachim K, et al. J Bacteriol, 2006 Dec. PMID 16997955, Free PMC Article
    4. Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme. Gao B, et al. Biochem Biophys Res Commun, 2005 Jun 17. PMID 15882995
    5. Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli. Quadroni M, et al. Eur J Biochem, 1996 Aug 1. PMID 8774726

    See all (15) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on complete protein
      Title: Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli.
    2. preliminary X-ray crystallographic studies
      Title: Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli.
    3. To determine the effects of protein interactions on catalysis, the steady-state kinetic parameters for SsuE were determined in single-enzyme assays and in the presence of the monooxygenase enzyme and alkanesulfonate substrate
      Title: Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables FMN reductase (NAD(P)H) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables FMN reductase (NAD(P)H) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables FMN reductase (NADPH) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within DNA damage response IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in alkanesulfonate catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in alkanesulfonate catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within alkanesulfonate catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within cellular response to sulfate starvation IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of FMN reductase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of FMN reductase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    NADPH-dependent FMN reductase
    NP_415457.1

    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
      996937..997512 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415457.1 NADPH-dependent FMN reductase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415457.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A6N8QUT4
      Conserved Domains (1) summary
      PRK10569
      Location:1 → 191
      PRK10569; NAD(P)H-dependent FMN reductase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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