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

• 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
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00139a024

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.