ABSTRACT
The nucleotide sequence of a 10,772 base pair (bp) region from Desulfovibrio gigas genome was determined. This sequence, which is adjacent to the region containing the coding units for the metalloproteins rubredoxin-oxygen oxidoreductase (ROO) and rubredoxin, includes the flavodoxin gene. Additionally, it also contains four open reading frames (ORFs) related to genes frequently found in replication origin regions of prokaryotes. These hypothetical encoded polypeptides are: the response regulator proteins (PhoP and PhoR) from the phosphate regulon, a DNA partitioning protein and an asparagine synthetase.
Subject(s)
DNA, Bacterial , Desulfovibrio/genetics , Genome, Bacterial , Replication Origin , Amino Acid Sequence , Aspartate-Ammonia Ligase/genetics , Bacterial Proteins/genetics , Flavodoxin/genetics , Genes, Bacterial , Molecular Sequence Data , Sequence Homology, Amino AcidABSTRACT
Sulfate-reducing bacteria are rich in unique redox proteins and electron carriers that participate in a variety of essential pathways. Several studies have been carried out to characterize these proteins, but the structure and function of many are poorly understood. Many Desulfovibrio species can grow using hydrogen as the sole energy source, indicating that the oxidation of hydrogen with sulfite as the terminal electron acceptor is an energy-conserving mechanism. Flavoredoxin is an FMN-binding protein isolated from the sulfate-reducing bacteria Desulfovibrio gigas that participates in the reduction of bisulfite from hydrogen. Here we report the cloning and sequencing of the flavoredoxin gene. The derived amino acid sequence exhibits similarity to several flavoproteins which are members of a new family of flavin reductases suggested to bind FMN in a novel mode.
