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tynA copper-containing amine oxidase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945939, updated on 4-Apr-2024

Summary

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Gene symbol
tynA
Gene description
copper-containing amine oxidase
Primary source
ASAP:ABE-0004639
Locus tag
b1386
See related
ECOCYC:EG13139
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
ECK1383; feaA; maoA
Summary
Topaquinone (TPQ) is 2,4,5-trihydroxyphenylalanine quinone, and is derived from a tyrosyl residue in the active site, in a copper-dependent oxidation reaction. [More information is available at EcoGene: EG13140].
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Genomic context

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Sequence:
NC_000913.3 (1449076..1451349, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional activator FeaR Neighboring gene phenylacetaldehyde dehydrogenase Neighboring gene fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase Neighboring gene phenylacetyl-CoA 1,2-epoxidase, monooxygenase subunit

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. Tyrosine 381 in E. coli copper amine oxidase influences substrate specificity. Kurtis CR, et al. J Neural Transm (Vienna), 2011 Jul. PMID 21547391
  2. Structure of a xenon derivative of Escherichia coli copper amine oxidase: confirmation of the proposed oxygen-entry pathway. Pirrat P, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008 Dec 1. PMID 19052360, Free PMC Article
  3. Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase. Mure M, et al. Biochemistry, 2005 Feb 8. PMID 15683241
  4. Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine. Wilmot CM, et al. FEBS Lett, 2004 Oct 22. PMID 15498552
  5. The multi-functional topa-quinone copper amine oxidases. Klinman JP. Biochim Biophys Acta, 2003 Apr 11. PMID 12686122

See all (38) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Only strains that produce TynA and FeaB converting norepinephrine to 3,4-dihydroxymandelic acid xhibited chemotaxis toward norepinephrine and 3,4-dihydroxymandelic acid is sensed by the serine chemoreceptor Tsr.
    Title: Chemotaxis of Escherichia coli to norepinephrine (NE) requires conversion of NE to 3,4-dihydroxymandelic acid.
  2. Using genetic, biochemical and computational approaches, authors show that the FeaR binding site is a TGNCA-N8-AAA motif that occurs in 2 copies in the tynA and feaB promoters.
    Title: Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli.
  3. proposed that Y381, together with another residue Y387, may be considered of critical importance for the substrate selectivity of copper amine oxidase through stacking or hydrophobic interactions with substrate
    Title: Tyrosine 381 in E. coli copper amine oxidase influences substrate specificity.
  4. N-terminus verified by Edman degradation on mature peptide
    Title: 2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression.
  5. X-ray crystal structure of the copper-containing quinoprotein amine oxidase determined in complex with the antidepressant drug tranylcypromine.
    Title: Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine.
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 aliphatic amine oxidase activity IEA
Inferred from Electronic Annotation
more info
  
enables calcium ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables copper ion binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables copper ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables primary amine oxidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables primary amine oxidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables primary amine oxidase activity IEA
Inferred from Electronic Annotation
more info
  
enables quinone binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables quinone binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in L-phenylalanine catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in amine metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in amine metabolic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within phenylethylamine catabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within phenylethylamine catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
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
copper-containing amine oxidase
NP_415904.3

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
    1449076..1451349 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415904.3 copper-containing amine oxidase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415904.3

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376WYY1, A0A8T5YGT1
    Conserved Domains (1) summary
    PRK14696
    Location:37 → 757
    tynA; primary-amine oxidase
Nucleotide Protein
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