Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)

Marc S Cortese; Allan B Caplan; Ronald L Crawford

doi:10.1186/1471-2148-2-8

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Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)

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Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)

Marc S Cortese, Allan B Caplan and Ronald L Crawford

BMC evolutionary biology, Vol.2(1), pp.8-8

04/23/2002

DOI: https://doi.org/10.1186/1471-2148-2-8

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https://hdl.handle.net/2376/111646

PMCID: PMC115864

PMID: 11972321

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Abstract

Protein Structure, Tertiary

Amino Acid Sequence

Genes, Bacterial - genetics

Virulence

Bacterial Proteins - chemistry

Bacterial Proteins - genetics

Molecular Sequence Data

Pseudomonas - pathogenicity

Gene Transfer, Horizontal

Pseudomonas - enzymology

Pyridines - metabolism

Conserved Sequence

Bacterial Proteins - metabolism

Pseudomonas - genetics

Pseudomonas - metabolism

Evolution, Molecular

Pyridine-2,6-bis(thiocarboxylic acid) (pdtc) is a small secreted metabolite that has a high affinity for transition metals, increases iron uptake efficiency by 20% in Pseudomonas stutzeri, has the ability to reduce both soluble and mineral forms of iron, and has antimicrobial activity towards several species of bacteria. Six GenBank sequences code for proteins similar in structure to MoeZ, a P. stutzeri protein necessary for the synthesis of pdtc. Analysis of sequences similar to P. stutzeri MoeZ revealed that it is a member of a superfamily consisting of related but structurally distinct proteins that are members of pathways involved in the transfer of sulfur-containing moieties to metabolites. Members of this family of enzymes are referred to here as MoeB, MoeBR, MoeZ, and MoeZdR. MoeB, the molybdopterin synthase activating enzyme in the molybdopterin cofactor biosynthesis pathway, is the most characterized protein from this family. Remarkably, lengths of greater than 73% nucleic acid homology ranging from 35 to 486 bp exist between Pseudomonas stutzeri moeZ and genomic sequences found in some Mycobacterium, Mesorhizobium, Pseudomonas, Streptomyces, and cyanobacteria species. The phylogenetic relationship among moeZ sequences suggests that P. stutzeri may have acquired moeZ through lateral gene transfer from a donor more closely related to mycobacteria and cyanobacteria than to proteobacteria. The importance of this relationship lies in the fact that pdtc, the product of the P. stutzeri pathway that includes moeZ, has an impressive set of capabilities, some of which could make it a potent pathogenicity factor.

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Title: Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)
Creators: Marc S Cortese - Environmental Research Institute, University of Idaho, Moscow, ID 83844-1052, USA. mcortese@uidaho.edu
Allan B Caplan
Ronald L Crawford
Publication Details: BMC evolutionary biology, Vol.2(1), pp.8-8
Academic Unit: UNKNOWN
Publisher: England
Identifiers: 99900547337401842
Language: English
Resource Type: Journal article