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cysJ [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947239, updated on 24-Aug-2024

Summary

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Official Symbol
cysJ
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].
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Genomic context

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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

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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. Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli. Sibille N, et al. Biochemistry, 2005 Jun 28. PMID 15966732
  2. Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain. Champier L, et al. Biochemistry, 2002 Mar 19. PMID 11888295
  3. 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
  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. 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

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

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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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

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Preferred Names
sulfite reductase, flavoprotein subunit
NP_417244.1

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
    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
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