Bacterioferritin

Details

Name
Bacterioferritin
Synonyms
  • 1.16.3.1
  • BFR
Gene Name
bfr
Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Amino acid sequence
>lcl|BSEQ0011219|Bacterioferritin
MAGNREDRKAKVIEVLNKARAMELHAIHQYMNQHYSLDDMDYGELAANMKLIAIDEMRHA
ENFAERIKELGGEPTTQKEGKVVTGQAVPVIYESDADQEDATIEAYSQFLKVCKEQGDIV
TARLFERIIEEEQAHLTYYENIGSHIKNLGDTYLAKIAGTPSSTGTASKGFVTATPAAE
Number of residues
179
Molecular Weight
19881.14
Theoretical pI
4.74
GO Classification
Functions
ferric iron binding / ferroxidase activity
Processes
intracellular sequestering of iron ion / iron ion transport
Components
cell
General Function
Ferroxidase activity
Specific Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011220|Bacterioferritin (bfr)
ATGGCTGGAAATAGAGAAGACCGCAAGGCCAAGGTCATCGAGGTTCTCAACAAGGCTCGC
GCCATGGAGCTGCACGCCATCCACCAATACATGAACCAGCACTATAGCCTGGATGACATG
GACTATGGTGAGCTTGCCGCCAACATGAAGCTTATTGCCATCGACGAGATGCGCCATGCG
GAAAACTTCGCCGAGCGTATCAAAGAACTGGGCGGCGAACCTACCACCCAGAAAGAAGGC
AAGGTGGTTACCGGACAGGCTGTGCCCGTTATCTACGAAAGCGATGCGGACCAGGAAGAC
GCCACCATCGAGGCGTACAGTCAATTTCTCAAGGTCTGTAAGGAACAGGGCGATATCGTC
ACTGCCCGTCTTTTCGAGCGCATTATTGAAGAAGAACAGGCCCATCTGACATATTACGAA
AATATCGGCAGCCATATCAAAAATCTGGGCGACACGTATCTGGCAAAGATTGCCGGTACG
CCATCGTCCACAGGAACTGCCAGCAAGGGCTTTGTTACCGCTACTCCGGCTGCTGAATAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ93PP9
UniProtKB Entry NameBFR_DESDA
GenBank Protein ID14326006
GenBank Gene IDAF321851
General References
  1. da Costa PN, Romao CV, LeGall J, Xavier AV, Melo E, Teixeira M, Saraiva LM: The genetic organization of Desulfovibrio desulphuricans ATCC 27774 bacterioferritin and rubredoxin-2 genes: involvement of rubredoxin in iron metabolism. Mol Microbiol. 2001 Jul;41(1):217-27. [Article]
  2. Romao CV, Regalla M, Xavier AV, Teixeira M, Liu MY, Le Gall J: A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans ATCC 27774. Biochemistry. 2000 Jun 13;39(23):6841-9. [Article]
  3. Romao CV, Louro R, Timkovich R, Lubben M, Liu MY, LeGall J, Xavier AV, Teixeira M: Iron-coproporphyrin III is a natural cofactor in bacterioferritin from the anaerobic bacterium Desulfovibrio desulfuricans. FEBS Lett. 2000 Sep 1;480(2-3):213-6. [Article]
  4. Coelho AV, Macedo S, Matias PM, Thompson AW, LeGall J, Carrondo MA: Structure determination of bacterioferritin from Desulfovibrio desulfuricans by the MAD method at the Fe K-edge. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):326-9. [Article]
  5. Macedo S, Romao CV, Mitchell E, Matias PM, Liu MY, Xavier AV, LeGall J, Teixeira M, Lindley P, Carrondo MA: The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans. Nat Struct Biol. 2003 Apr;10(4):285-90. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails