Biological Nitrogen Removal Database

A manually curated data resource for microbial nitrogen removal


Detailed information

Microorganism

Desulfovibrio desulfuricans strain (ATCC 27774 / DSM 6949 / MB)

Taxonomy

  • Phylum : Proteobacteria
  • Class : Deltaproteobacteria
  • Order : Desulfovibrionales
  • Family : Desulfovibrionaceae
  • Genus : Desulfovibrio

Isolation Source

nan

Enzyme Name

napC protein

  • Encoding Gene:napC
  • DNA Size:5190 bp
  • Nucleotide FASTA sequence: Link

  • UniProt I.D: Q599H0

Protein Information

  • Pro_GenBank I.D: CAI72601.1

  • Length:190 aa
  • Protein FASTA_sequence: Link

Information about Article

  • Reference:Marietou et al., 2005
  • Title:Nitrate reduction by Desulfovibrio desulfuricans: a periplasmic nitrate reductase system that lacks NapB, but includes a unique tetraheme c-type cytochrome, NapM
  • Pubmed ID:15972253.0
  • Pubmed link: Link

  • Full research link: Link

  • Abstract:Many sulphate reducing bacteria can also reduce nitrite, but relatively few isolates are known to reduce nitrate. Although nitrate reductase genes are absent from Desulfovibrio vulgaris strain Hildenborough, for which the complete genome sequence has been reported, a single subunit periplasmic nitrate reductase, NapA, was purified from Desulfovibrio desulfuricans strain 27774, and the structural gene was cloned and sequenced. Chromosome walking methods have now been used to determine the complete sequence of the nap gene cluster from this organism. The data confirm the absence of a napB homologue, but reveal a novel six-gene organisation, napC-napM-napA-napD-napG-napH. The NapC polypeptide is more similar to the NrfH subgroup of tetraheme cytochromes than to NapC from other bacteria. NapM is predicted to be a tetra-heme c-type cytochrome with similarity to the small tetraheme cytochromes from Shewanella oneidensis. The operon is located close to a gene encoding a lysyl-tRNA synthetase that is also found in D. vulgaris. We suggest that electrons might be transferred to NapA either from menaquinol via NapC, or from other electron donors such as formate or hydrogen via the small tetraheme cytochrome, NapM. We also suggest that, despite the absence of a twin-arginine targeting sequence, NapG might be located in the periplasm where it would provide an alternative direct electron donor to NapA.