U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    cysJ sulfite reductase, flavoprotein subunit [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947239, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    cysJ
    Official Full Name
    sulfite reductase, flavoprotein subunit
    Primary source
    ECOCYC:EG10191
    Locus tag
    b2764
    See related
    ASAP:ABE-0009063
    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
    ECK2759
    Summary
    The subunit binds one FMN and one FAD per chain. [More information is available at EcoCyc: EG10191].
    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 (2890099..2891898, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene phosphoadenosine phosphosulfate reductase Neighboring gene sulfite reductase, hemoprotein subunit Neighboring gene 6-carboxy-5,6,7,8-tetrahydropterin synthase Neighboring gene putative oxidoreductase with FAD/NAD(P)-binding domain Neighboring gene putative 4Fe-4S cluster-containing 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. Molecular characterization of the cysJIH promoters of Salmonella typhimurium and Escherichia coli: regulation by cysB protein and N-acetyl-L-serine. Ostrowski J, et al. J Bacteriol, 1989 Jan. PMID 2701932, Free PMC Article
    2. The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis. Gruez A, et al. Acta Crystallogr D Biol Crystallogr, 1998 Jan 1. PMID 9761836
    3. 31P nuclear magnetic resonance study of the flavoprotein component of the Escherichia coli sulfite reductase. Evrard A, et al. Eur J Biochem, 1999 Apr. PMID 10215853
    4. Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride. Covès J, et al. Biochem J, 1999 Sep 1. PMID 10455035, Free PMC Article
    5. Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. Gruez A, et al. J Mol Biol, 2000 May 26. PMID 10860732

    See all (50) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase.
      Title: Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase.
    2. A model is proposed for the inhibition of growth in which the reduction of furfural by YqhD enzyme depletes NADPH sufficiently to limit the assimilation of sulfur into amino acids (cysteine and methionine) by CysIJ (sulfite reductase).
      Title: Furfural inhibits growth by limiting sulfur assimilation in ethanologenic Escherichia coli strain LY180.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: Mutagenesis and regulation of the cysJ promoter of 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 FMN binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables FMN binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables FMN binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables NADP+ binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables flavin adenine dinucleotide binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables flavin adenine dinucleotide binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables flavin adenine dinucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables flavin adenine dinucleotide binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables oxidoreductase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables riboflavin reductase (NADPH) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables sulfite reductase (NADPH) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cysteine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cysteine biosynthetic process NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in hydrogen sulfide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in sulfate assimilation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in sulfate assimilation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of sulfite reductase complex (NADPH) IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of sulfite reductase complex (NADPH) IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    sulfite reductase, flavoprotein subunit
    NP_417244.1

    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
      2890099..2891898 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417244.1 sulfite reductase, flavoprotein subunit [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417244.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8T5Y9L7
      Conserved Domains (1) summary
      PRK10953
      Location:1 → 599
      cysJ; NADPH-dependent assimilatory sulfite reductase flavoprotein subunit
    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.