Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases

We have deduced the nucleotide sequence of the genes encoding the three components of 4-chlorobenzoate (4-CBA) dehalogenase from Pseudomonas sp. CBS-3 and examined the origin of these proteins by homology analysis. Open reading frame 1 (ORF1) encodes a 30-kDa 4-CBA-coenzyme A dehalogenase related to...

Full description

Saved in:

Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 31; no. 24; pp. 5594 - 5604
Main Authors:	Babbitt, Patricia C, Kenyon, George L, Martin, Brian M, Charest, Hugues, Slyvestre, Michel, Scholten, Jeffrey D, Chang, Kai Hsuan, Liang, Po Huang, Dunaway-Mariano, Debra
Format:	Journal Article
Language:	English
Published:	Washington, DC American Chemical Society 01-06-1992
Subjects:	4-chlorobenzoate dehalogenase Amino Acid Sequence Animals Bacteriology Base Sequence Biological and medical sciences Biological Evolution Fundamental and applied biological sciences. Psychology genes Genes, Bacterial Hydrolases - chemistry Hydrolases - genetics Hydrolases - metabolism Ligases - chemistry Ligases - genetics Metabolism. Enzymes Microbiology Molecular Sequence Data nucleotide sequence Palmitoyl-CoA Hydrolase - chemistry Palmitoyl-CoA Hydrolase - genetics predictions Pseudomonas Pseudomonas - enzymology Sequence Alignment Pseudomonadales Enoyl-CoA hydratase Molecular evolution Nucleotide sequence Enzyme Bacteria Pseudomonadaceae Gene organization Pseudomonas Aminoacid sequence
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	We have deduced the nucleotide sequence of the genes encoding the three components of 4-chlorobenzoate (4-CBA) dehalogenase from Pseudomonas sp. CBS-3 and examined the origin of these proteins by homology analysis. Open reading frame 1 (ORF1) encodes a 30-kDa 4-CBA-coenzyme A dehalogenase related to enoyl-coenzyme A hydratases functioning in fatty acid beta-oxidation. ORF2 encodes a 57-kDa protein which activates 4-CBA by acyl adenylation/thioesterification. This 4-CBA:coenzyme A ligase shares significant sequence similarity with a large group of proteins, many of which catalyze similar chemistry in beta-oxidation pathways or in siderophore and antibiotic synthetic pathways. These proteins have in common a short stretch of sequence, (T,S)(S,G)G(T,S)(T,E)G(L,X)PK(G,-), which is particularly highly conserved and which may represent an important new class of "signature" sequence. We were unable to find any proteins homologous in sequence to the 16-kDa 4-hydroxybenzoate-coenzyme A thioesterase encoded by ORF3. Analysis of the chemistry and function of the proteins found to be structurally related to the 4-CBA:coenzyme A ligase and the 4-CBA-coenzyme A dehalogenase supports the proposal that they evolved from a beta-oxidation pathway.
Bibliography:	istex:160CBBB6B3BF5624F747A536341B5578C4F6BAB8 ark:/67375/TPS-8ZS3GJTR-D ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi00139a024