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Eur J Biochem. 1998 Jun 1;254(2):325-32.

A family of flavoproteins in the domains Archaea and Bacteria.

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1
Mikrobiologisches Institut, Eidgenössische Technische Hochschule, Zürich, Switzerland. wasserfallen@micro.biol.ethz.ch

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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