Burkholderia dolosa AU0158, AK34_RS09175

Cytoplasmic
Cytoplasmic Membrane
Periplasmic
Outer Membrane
Extracellular
Unknown
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Gene Feature Overview

Strain Burkholderia dolosa AU0158 (complete genome)
GCF_000959505.1|latest
Locus Tag
AK34_RS09175
NCBI Old Locus TagAK34_4994
Name
Synonym: PaaZ-ECH
Synonym: BDAG_04127
Replicon chromosome 2
Genomic location 2102525 - 2102983 (- strand)
CommentIn E. coli, paaZ encodes a bifunctional protein consisting of an N-terminal NADP-dependent aldehyde dehydrogenase domain and a C-terminal MaoC-like (R)-specific enoyl-CoA hydratase domain. In Burkholderia genomes, a gene incorrectly annotated as paaZ (e.g WQ49_RS11500) encodes only one of the two domains found in E.coli paaZ (the domain with semialdehyde dehydrogenase activity) and so is renamed PacL (PMID:21296885) but was also referred to as PaaZ-ALDH in the manuscript. In the same study , a separate A. aromaticum, protein (UniProtKB:Q5P232) with the (R)-hydratase activity was annotated as Ech-Aa and the Burkholderia ortholog was annotated as PaaZ-ECH.

Cross-References

RefSeq WP_035974808.1
GI 738013427
NCBI Locus Tag AK34_RS09175
NCBI Old Locus Tag AK34_4994
RefSeq WP_035974808.1

Product

Feature Type CDS
Coding Frame 1
Product Name
putative (R)-specific oxepin-CoA hydratase
Product Name Confidence: Class 2
Synonyms acyl dehydratase
Evidence for Translation
Charge (pH 7) -0.63
Kyte-Doolittle Hydrophobicity Value -0.159
Molecular Weight (kDa) 16894.2
Isoelectric Point (pI) 6.79

Subcellular localization

Individual Mappings
Localization Confidence PMID
Cytoplasmic Class 3
Additional evidence for subcellular localization

AlphaFold 2 Protein Structure Predictions

Protein structure predictions using a neural network model developed by DeepMind. If a UniProtKB accession is associated with this protein, a search link will be provided below.

Pathogen Association Analysis

Results Analysis not done

Orthologs/Comparative Genomics

Burkholderia Ortholog Group BG005317 (313 members)
Putative Inparalogs None Found

Interactions

STRING database Search for predicted protein-protein interactions using:
Search term: AK34_RS09175

Human Homologs

References

Studies on the mechanism of ring hydrolysis in phenylacetate degradation: a metabolic branching point.
Teufel R, Gantert C, Voss M, Eisenreich W, Haehnel W, Fuchs G
J Biol Chem 2011 Apr 1;286(13):11021-34
PubMed ID: 21296885