Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases

Microbiology. 1995 Feb;141 ( Pt 2):449-58. doi: 10.1099/13500872-141-2-449.

Abstract

The hydBGDA genes, which encode the four subunits beta, gamma, delta and alpha of the [Ni-Fe] hydrogenase from the archaeon Pyrococcus furiosus, have been isolated and sequenced using a PCR/IPCR-based strategy. From the sequence analysis it appears that the four structural genes are tightly linked and organized in a single transcription unit. The hydD and hydA gene products are related to the small and the large subunits of several archaeal and eubacterial [Ni-Fe] hydrogenases with an overall degree of sequence relatedness ranging from 35% to 50% (identity + similarity). In particular, the amino acid sequence motifs involved in the accommodation of nickel and iron-sulfur clusters are conserved. In addition, the database search revealed that the hydB and hydG gene products are homologous to the asrA- and asrB-encoded subunits of the sulfite reductase enzyme from Salmonella typhimurium. This is particularly interesting in view of the recent finding that the P. furiosus hydrogenase appears to be a bifunctional enzyme endowed with both proton- and sulfur-reducing activities.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Archaea / enzymology
  • Archaea / genetics*
  • Base Sequence
  • Conserved Sequence
  • Genes, Bacterial / genetics*
  • Hydrogenase / genetics*
  • Hydrogenase / isolation & purification
  • Molecular Sequence Data
  • Multigene Family / genetics*
  • Oxidoreductases Acting on Sulfur Group Donors / genetics
  • Salmonella typhimurium / enzymology
  • Salmonella typhimurium / genetics
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • nickel-iron hydrogenase
  • Hydrogenase
  • Oxidoreductases Acting on Sulfur Group Donors

Associated data

  • GENBANK/X75255