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

Gene ID: 945939, updated on 30-Jul-2025
Official Symbol
tynA
Official Full Name
copper-containing amine oxidase
Primary source
ECOCYC:EG13139
Locus tag
b1386
See related
ASAP:ABE-0004639
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; 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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential. Murray JM, et al. Biochemistry, 2001 Oct 30. PMID 11669617
  2. Copper amine oxidase: a novel use for a tyrosine. Fontecave M, et al. Structure, 1995 Nov 15. PMID 8591022
  3. Intermediates in the catalytic cycle of copper-quinoprotein amine oxidase from Escherichia coli. Steinebach V, et al. J Biol Chem, 1996 Mar 8. PMID 8621418
  4. Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12. Roh JH, et al. J Mol Biol, 1994 May 13. PMID 8176752
  5. Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction. Wilmot CM, et al. Biochemistry, 1997 Feb 18. PMID 9048544

See all (37) 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
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
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 oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables primary methylamine oxidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables primary methylamine oxidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables primary methylamine 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
  
Preferred Names
copper-containing amine oxidase
NP_415904.3

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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

    See identical proteins and their annotated locations for NP_415904.3

    Status: REVIEWED

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