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azu azurin [ Pseudomonas aeruginosa PAO1 ]

Gene ID: 878046, updated on 30-Jul-2025
Gene symbol
azu
Gene description
azurin
Locus tag
PA4922
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Pseudomonas aeruginosa PAO1 (strain: PAO1)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas
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Sequence:
NC_002516.2 (5521664..5522110, complement)

NC_002516.2Genomic Context describing neighboring genes Neighboring gene NAD synthetase Neighboring gene hypothetical protein Neighboring gene hypothetical protein Neighboring gene hypothetical protein

Genomic Sequence:
NC_002516.2

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Reduction potential variations in azurin through secondary coordination sphere phenylalanine incorporations. Berry SM, et al. J Inorg Biochem, 2010 Oct. PMID 20615551
  2. The early steps in the unfolding of azurin. Rizzuti B, et al. Biochemistry, 2004 Dec 14. PMID 15581373
  3. Effects of a novel disulfide bond and engineered electrostatic interactions on the thermostability of azurin. Tigerström A, et al. Biochemistry, 2004 Oct 5. PMID 15449946
  4. Conformational changes in azurin from Pseudomona aeruginosa induced through chemical and physical protocols. Fuentes L, et al. Biophys J, 2004 Sep. PMID 15345565, Free PMC Article
  5. Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin. Marks J, et al. J Biol Inorg Chem, 2004 Apr. PMID 14758526

See all (31) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Review of activity of Pseudomonas aeruginosa azurin and azurin-like bacteriocins; including hijacking of key cellular regulators and cell surface receptors to remodel the cellular signaling networks.
    Title: Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy.
  2. this study shows that addition of Cys at position 78 modulates the functional shifting of this protein from a peroxidase to a chaperone
    Title: Enhancement of the Chaperone Activity of Alkyl Hydroperoxide Reductase C from Pseudomonas aeruginosa PAO1 Resulting from a Point-Specific Mutation Confers Heat Tolerance in Escherichia coli.
  3. Mercury metallation of the bacterial copper protein azurin is analogous to the one of human cerulopsmin and factor VIII in mercury poisoning.
    Title: Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity.
  4. Study presents the high-resolution (1.5 A) structure of azurin from Pseudomonas aeruginosa PAO1 spin labelled with MTSSL at position T21; due to the crystal-packing environment in the triclinic crystals, the label is observed in two different but fully ordered states.
    Title: High-resolution crystal structure of spin labelled (T21R1) azurin from Pseudomonas aeruginosa: a challenging structural benchmark for in silico spin labelling algorithms.
  5. Results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function.
    Title: Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7 Å.
  6. The study examines the spectral properties of tryptophan radicals in two azurin mutants (Az48W and ReAz108W).
    Title: Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin.
  7. Atomic force spectroscopy was used to investigate the interaction of p28 peptide fragment of azurin with full-length p53 and its isolated domains at the single molecule level.
    Title: Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy.
  8. structure of the active-site loop has a dramatic effect on the kinetic stability and the unfolding pathway
    Title: The influence of active site loop mutations on the thermal stability of azurin from Pseudomonas aeruginosa.
  9. Studies indicate that in the crystal structure of azurin the H20 is strongly hydrogen bonded to Y48 (2.7-2.8A tyrosine-O to histidine-N distance.
    Title: Redox properties of tyrosine and related molecules.
  10. Data show that almost all of the azurin variant potentials were shifted to higher values than WT azurin.
    Title: Reduction potential variations in azurin through secondary coordination sphere phenylalanine incorporations.
Submit: New GeneRIF Correction See all GeneRIFs (17)

Homology

Gene Ontology Provided by PseudoCAP

Function Evidence Code Pubs
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
  
enables copper ion binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables electron transfer activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables transition metal ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables zinc ion binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
azurin
NP_253609.1
  • Product name confidence: class 1 (Function experimentally demonstrated in P. aeruginosa)

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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_002516.2 Reference assembly

    Range
    5521664..5522110 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_253609.1 azurin [Pseudomonas aeruginosa PAO1]

    See identical proteins and their annotated locations for NP_253609.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A4Y6GMG4
    Conserved Domains (1) summary
    COG3241
    Location:23 → 148
    COG3241; Azurin [Energy production and conversion]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00282.2

Gene LinkOut

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Molecular Biology Databases
Research Materials