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
- Functionsferric iron binding / ferroxidase activityProcessesintracellular sequestering of iron ion / iron ion transportComponentscell
- 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
- Ferritin (PF00210)
- 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
Resource Link UniProtKB ID Q93PP9 UniProtKB Entry Name BFR_DESDA GenBank Protein ID 14326006 GenBank Gene ID AF321851 - General References
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details