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      A family of flavoproteins in the domains Archaea and Bacteria.

      European journal of biochemistry / FEBS
      Amino Acid Sequence, Archaeal Proteins, chemistry, classification, genetics, Bacterial Proteins, Base Sequence, Cloning, Molecular, Cyanobacteria, DNA Primers, DNA, Archaeal, DNA, Bacterial, Desulfovibrio, Escherichia coli, Flavoproteins, Mixed Function Oxygenases, Molecular Sequence Data, Recombinant Proteins, Rhodobacter capsulatus, Rubredoxins, Sequence Homology, Amino Acid

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          Abstract

          A family of flavoproteins, called A-type flavoproteins, is described. It consists of 14 protein sequences of 385-597 amino acids in length, 7 from methanogens (domain: Archaea), 5 from phototrophic prokaryotes, one from Escherichia coli, and a partial sequence from the sulfate reducer Desulfovibrio gigas (domain: Bacteria). No similar sequence could be found in the domain Eucarya. All sequences show significant similarity over a 385-400 amino acid portion overlapping a recognizable flavodoxin signature starting at positions 245-285 of the common core sequence. Cofactor analysis and, to some extent, analysis of the primary structure of six A-type flavoproteins, three of which are structurally characterized here, support the existence of four sub-families: (a) simple flavoproteins binding only FMN; (b) diflavin flavoproteins binding FMN and FAD; (c) a flavorubredoxin binding FMN and iron; (d) a hemoflavoprotein. The possible involvement of A-type flavoproteins in the metabolism of oxygen, as suggested for D. gigas hemoflavoprotein [Gomes, C. M., Silva, G., Oliveira, S., LeGall, J., Liu, M.-Y., Xavier, A. V., Rodrigues-Pousada, C. & Teixeira, M. (1997) J. Biol. Chem. 272, 22502-22508], is discussed.

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