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cueO multicopper oxidase CueO [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947736, updated on 3-Dec-2024

Summary

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Official Symbol
cueO
Official Full Name
multicopper oxidase CueO
Primary source
ECOCYC:EG12318
Locus tag
b0123
See related
ASAP:ABE-0000430
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
ECK0122; yacK
Summary
Verified Tat substrate: [More information is available at EcoGene: EG12318]. CueO multicopper oxidase is a copper-stimulated phenoloxidase and ferroxidase that plays a role in copper homeostasis during aerobiosis . [More information is available at EcoCyc: EG12318].
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Genomic context

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Sequence:
NC_000913.3 (137083..138633)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene spermidine synthase Neighboring gene putative lipoprotein YacC Neighboring gene quinoprotein glucose dehydrogenase Neighboring gene hypoxanthine phosphoribosyltransferase

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 structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity. Wang H, et al. Sci Rep, 2018 Sep 24. PMID 30250139, Free PMC Article
  2. CuiD is a crucial gene for survival at high copper environment in Salmonella enterica serovar Typhimurium. Lim SY, et al. Mol Cells, 2002 Oct 31. PMID 12442888
  3. A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO. Roberts SA, et al. J Biol Chem, 2003 Aug 22. PMID 12794077
  4. Sequential reconstitution of copper sites in the multicopper oxidase CueO. Galli I, et al. J Biol Inorg Chem, 2004 Jan. PMID 14648285
  5. Cuprous oxidase activity of CueO from Escherichia coli. Singh SK, et al. J Bacteriol, 2004 Nov. PMID 15516598, Free PMC Article

See all (57) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes.
    Title: Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes.
  2. The cuprous oxidase activity of these mutants was about 20% that of wild-type CueO. These structural features of the G304K mutant provide clues for designing specific substrate-binding mutants in the biotechnological applications.
    Title: Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity.
  3. Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO has been presented.
    Title: Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO prepared from a new expression construct for neutron crystallography.
  4. Exogenous acetate ion reaches the type II copper center in CueO through the water-excretion channel and potentially affects the enzymatic activity.
    Title: Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity.
  5. the binding of copper to apo-CueO greatly stabilized the protein, indicating a transformation from an open or flexible domain arrangement with accessible copper sites to a closed structure with deeply buried copper ions.
    Title: The Tat Substrate CueO Is Transported in an Incomplete Folding State.
  6. The results provides evidence that CueO possesses high Mn(II) oxidase activity and generates biogenic Mn oxide gamma-Mn3O4.
    Title: Catalytic oxidation of manganese(II) by multicopper oxidase CueO and characterization of the biogenic Mn oxide.
  7. At low levels of X-ray exposure, unambiguous electron density for an O atom is observed inside the trinuclear copper center (TNC); binding of oxygen to the TNC after its full reduction is observed in the case of the laccase.
    Title: New insights into the catalytic active-site structure of multicopper oxidases.
  8. Laccase activities of CueO were maximally enhanced 140-fold by virtue of the synergistic effect of mild mutations at and at around the ligand groups to type I copper.
    Title: Modifications of laccase activities of copper efflux oxidase, CueO by synergistic mutations in the first and second coordination spheres of the type I copper center.
  9. These results exerted on the hydrogen bond network in CueO are discussed in comparison with proton transfers in cytochrome oxidase.
    Title: Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities.
  10. The results revealed that the crude CueO catalyzed the oxidation of anthracene and benzo[a]pyrene in the same way as the fungal laccase from Trametes versicolor, but showed specific characteristics such as thermostability and copper dependence.
    Title: Oxidation of polycyclic aromatic hydrocarbons by the bacterial laccase CueO from E. coli.
Submit: New GeneRIF Correction See all GeneRIFs (15)

Pathways from PubChem

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General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables copper ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
  
enables copper ion binding ISM
Inferred from Sequence Model
more info
 PubMed 
enables ferroxidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ferroxidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor IDA
Inferred from Direct Assay
more info
 PubMed 
enables oxidoreductase activity, acting on metal ions IDA
Inferred from Direct Assay
more info
 PubMed 
enables oxidoreductase activity, acting on metal ions, oxygen as acceptor IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within detoxification of copper ion IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within response to copper ion IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within response to copper ion IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in outer membrane-bounded periplasmic space IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
multicopper oxidase CueO
NP_414665.1

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
    137083..138633
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414665.1 multicopper oxidase CueO [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414665.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7E955, F4NAQ7
    Conserved Domains (1) summary
    PRK10965
    Location:1 → 516
    PRK10965; multicopper oxidase; Provisional
Nucleotide Protein
Heading Accession and Version

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