PMID:2334437

Citation	Helms, LR, Krey, GD and Swenson, RP (1990) Identification, sequence determination, and expression of the flavodoxin gene from Desulfovibrio salexigens. Biochem. Biophys. Res. Commun. 168:809-17
Abstract	Restriction fragments of genomic DNA from Desulfovibrio salexigens (ATCC 14822) containing the structural gene coding for the flavodoxin protein were identified using the entire coding region of the gene for the Desulfovibrio vulgaris (Hildenborough) flavodoxin as a probe (Krey, G.D., Vanin, E.F., and Swenson, R.P. (1988) J. Biol. Chem. 263, 15436-15443). A 1.4-kb PstI-HindIII fragment was ultimately identified which contains an open reading frame coding for a polypeptide of 146 amino acid residues that was highly homologous to the D. vulgaris flavodoxin, sharing a sequence identity of 55%. When compared to the X-ray crystal structure of the D. vulgaris protein, the homologous regions were largely confined to those portions of the protein which are in the immediate vicinity of the flavin mononucleotide cofactor binding site. Tryptophan-60 and tyrosine-98, which reside on either side of the isoalloxazine ring of the cofactor, are conserved, as are the sequences of the polypeptide loop that interacts with the phosphate moiety of the flavin. Acidic residues forming the interface of model electron-transfer complexes with certain cytochrome c proteins are retained. The flavodoxin holoprotein is over-expressed in E. coli from the cloned gene using its endogenous promoter.
Links	PubMed
Keywords	Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA, Bacterial/biosynthesis; Desulfovibrio/genetics; Flavodoxin/genetics; Flavoproteins/genetics; Gene Expression; Genes, Bacterial; Molecular Sequence Data; Restriction Mapping
edit table

Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
DESAD:FLAV		GO:0009055: electron carrier activity	ECO:0000247:	UniProtKB:P00323	F		Matched 100% with Flavodoxin; electron transport (4HEQ - the crystal structure of flavodoxin from Desulfovibrio gigas) with an E-value of 7.6E-30. Figure 4 of the PubMed article compares the flavodoxin protein sequences found in D. vulgaris and D. salexigens. Most protein sequences compared between the two were found to be identical (marked with a ";") or conservative (marked with a ":"), showing much similarity between what was found between the two. This provides evidence that flavodoxin appears in D. salexigens as it does in D. vulgaris. Additionally, Page 814 of the article adds more evidence to the fact that when the X-ray structure of the DVF was compared, all homologous regions were confined to areas in which were in the immediate vicinity of the flavin mononucleotide cofactor binding site. It was stated that all known flavodoxin structures provided highly conserved sequences near an amino terminus which surrounds the hydrogen bonds of the cofactor. This additionally shows evidence of the presence of flavodoxin in D. salexigens as it appears in D. vulgaris.	complete CACAO 11885

References

See Help:References for how to manage references in GONUTS.