U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

paaD phenylacetate degradation protein [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945959, updated on 19-Sep-2024

Summary

Go to the top of the page Help
Official Symbol
paaD
Official Full Name
phenylacetate degradation protein
Primary source
ECOCYC:G6712
Locus tag
b1391
See related
ASAP:ABE-0004655
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
ECK1388; ydbQ
Summary
PaaABCDE is a multi-subunit oxygenase that hydroxylates phenylacetyl-CoA. [More information is available at EcoGene: EG13738]. PaaA, PaaB, PaaC, and PaaD are predicted to be subunits of a phenylacetate-CoA oxygenase involved in phenylacetate catabolism . [More information is available at EcoCyc: G6712].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Sequence:
NC_000913.3 (1455925..1456422)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene phenylacetyl-CoA 1,2-epoxidase subunit B Neighboring gene phenylacetyl-CoA 1,2-epoxidase, structural subunit Neighboring gene phenylacetyl-CoA 1,2-epoxidase, reductase subunit Neighboring gene putative 2,3-dehydroadipyl-CoA hydratase Neighboring gene putative ring 1,2-epoxyphenylacetyl-CoA isomerase (oxepin-CoA forming)

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the aerobic phenylacetic acid degradation pathway of Escherichia coli. Fernández C, et al. Appl Environ Microbiol, 2006 Nov. PMID 16997993, Free PMC Article
  2. Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli. Ismail W, et al. Eur J Biochem, 2003 Jul. PMID 12846838
  3. Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli. Ferrández A, et al. J Biol Chem, 2000 Apr 21. PMID 10766858
  4. The binary protein-protein interaction landscape of Escherichia coli. Rajagopala SV, et al. Nat Biotechnol, 2014 Mar. PMID 24561554, Free PMC Article
  5. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. Ferrández A, et al. J Biol Chem, 1998 Oct 2. PMID 9748275

See all (8) citations in PubMed

GeneRIFs: Gene References Into Functions

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by EcoCyc

Process Evidence Code Pubs
involved_in phenylacetate catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in phenylacetate catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
phenylacetate degradation protein

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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
    1455925..1456422
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415909.4 phenylacetate degradation protein [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415909.4

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8T5ZYZ8
    Conserved Domains (1) summary
    TIGR02159
    Location:22 → 165
    PA_CoA_Oxy4; phenylacetate-CoA oxygenase, PaaJ subunit
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.