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fdoG formate dehydrogenase O subunit alpha [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948394, updated on 4-Apr-2024

Summary

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Gene symbol
fdoG
Gene description
formate dehydrogenase O subunit alpha
Primary source
ASAP:ABE-0012710
Locus tag
b3894
See related
ECOCYC:EG11858
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
ECK3887
Summary
Also known as FDH-Z. [More information is available at EcoGene: EG11858]. By similarity to the paralogous subunit of formate dehydrogenase-N, FdnG, FdoG is thought to be the catalytic subunit of formate dehydrogenase-O, containing the bis-molybdopterin guanine dinucleotide (MGD) cofactor and selenocysteine . [More information is available at EcoCyc: EG11858].
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Genomic context

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Sequence:
NC_000913.3 (4082772..4085822, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene formate dehydrogenase formation protein Neighboring gene formate dehydrogenase O subunit gamma Neighboring gene formate dehydrogenase O subunit beta Neighboring gene sulfurtransferase for molybdenum cofactor sulfuration Neighboring gene DUF3829 domain-containing lipoprotein YiiG

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. SECISDesign: a server to design SECIS-elements within the coding sequence. Busch A, et al. Bioinformatics, 2005 Aug 1. PMID 15919727
  2. An algorithm for identification of bacterial selenocysteine insertion sequence elements and selenoprotein genes. Zhang Y, et al. Bioinformatics, 2005 Jun 1. PMID 15797911
  3. Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide. Barker HC, et al. Mol Microbiol, 2000 Mar. PMID 10760151
  4. Expression and operon structure of the sel genes of Escherichia coli and identification of a third selenium-containing formate dehydrogenase isoenzyme. Sawers G, et al. J Bacteriol, 1991 Aug. PMID 1650339, Free PMC Article
  5. Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates. Chan CS, et al. FEBS Lett, 2010 Nov 19. PMID 20974141, Free PMC Article

See all (31) citations in PubMed

GeneRIFs: Gene References Into Functions

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 4 iron, 4 sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
  
enables electron transfer activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables electron transfer activity IEA
Inferred from Electronic Annotation
more info
  
enables formate dehydrogenase (NAD+) activity IEA
Inferred from Electronic Annotation
more info
  
enables formate dehydrogenase (cytochrome-c-553) activity IEA
Inferred from Electronic Annotation
more info
  
enables formate dehydrogenase (quinone) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables iron-sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
  
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 molybdopterin cofactor binding 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 
Process Evidence Code Pubs
acts_upstream_of_or_within DNA damage response IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in anaerobic electron transport chain NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in anaerobic respiration IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in cellular respiration IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within cellular respiration IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within formate oxidation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in formate oxidation NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in heme oxidation NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of formate dehydrogenase complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of formate dehydrogenase complex ISS
Inferred from Sequence or Structural Similarity
more info
  
located_in membrane HDA PubMed 
located_in membrane ISS
Inferred from Sequence or Structural Similarity
more info
  
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane HDA PubMed 

General protein information

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Preferred Names
formate dehydrogenase O subunit alpha
NP_418330.1

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
    4082772..4085822 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418330.1 formate dehydrogenase O subunit alpha [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418330.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7YKH3
    Conserved Domains (1) summary
    cl09928
    Location:2 → 1015
    Molybdopterin-Binding; Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and ...
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases