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Literature summary for 1.18.6.2 extracted from

  • Robson, R.; Woodley, P.; Pau, R.; Eady, R.
    Structural genes for the vanadium nitrogenase from Azotobacter chroococcum (1989), EMBO J., 8, 1217-1224 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.6.2

Organism

Organism UniProt Comment Textmining
Azotobacter chroococcum P15332 and P15334 and P15333 P15332 i.e. subunit VnfD, P15334 i.e. subunit VnfK, P15333 i.e. subunit VnfG
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Azotobacter chroococcum MCD1 P15332 and P15334 and P15333 P15332 i.e. subunit VnfD, P15334 i.e. subunit VnfK, P15333 i.e. subunit VnfG
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Subunits

Subunits Comment Organism
? x * 53793, subunit VnfD, x * 52724, subunit VnfK, x * 13274, subunit vnfG, calculated Azotobacter chroococcum

Synonyms

Synonyms Comment Organism
vnfD alpha-chain Azotobacter chroococcum
vnfG delta-chain Azotobacter chroococcum
vnfK beta-chain Azotobacter chroococcum

Expression

Organism Comment Expression
Azotobacter chroococcum genes for the three subunits vnJD (alpha), vnfG (delta) and vnfK (beta) are contiguous and form an operon whose transcription is repressed in response to ammonia additional information

General Information

General Information Comment Organism
physiological function a deletion in the VnfD, VnfG and VnfK gene cluster prevents V-dependent nitrogen fixation. A strain defective in both V-nitrogenase and Mo-nitrogenase (EC 1.18.6.1) structural genes shows no residual nitrogen fixing capacity Azotobacter chroococcum