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

Gene ID: 945947, updated on 10-Oct-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
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