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Q93PP9 (BFR_DESDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bacterioferritin

Short name=BFR
EC=1.16.3.1
Gene names
Name:bfr
Ordered Locus Names:Ddes_1387
OrganismDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) [Complete proteome] [HAMAP]
Taxonomic identifier525146 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Iron-storage protein, whose ferroxidase center binds Fe2+ ions, oxidizes them by dioxygen to Fe3+, and participates in the subsequent Fe3+ oxide mineral core formation within the central cavity of the protein complex.

Catalytic activity

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Cofactor

Binds 1 Fe-coproporphyrin III group per dimer. Ref.4

Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center. Ref.4

Subunit structure

Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited. Ref.3

Sequence similarities

Belongs to the bacterioferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179Bacterioferritin
PRO_0000192591

Regions

Domain1 – 150150Ferritin-like diiron

Sites

Metal binding231Iron 1 Ref.6
Metal binding561Iron 1 Ref.6
Metal binding561Iron 2 Ref.6
Metal binding571Iron (Fe-coproporphyrin III axial ligand); shared with dimeric partner Ref.6
Metal binding591Iron 1 Ref.6
Metal binding991Iron 2 Ref.6
Metal binding1321Iron 1 Ref.6
Metal binding1321Iron 2 Ref.6
Metal binding1351Iron 2 Ref.6

Secondary structure

........... 179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q93PP9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 09E3387462FED3A3

FASTA17919,881
        10         20         30         40         50         60 
MAGNREDRKA KVIEVLNKAR AMELHAIHQY MNQHYSLDDM DYGELAANMK LIAIDEMRHA 

        70         80         90        100        110        120 
ENFAERIKEL GGEPTTQKEG KVVTGQAVPV IYESDADQED ATIEAYSQFL KVCKEQGDIV 

       130        140        150        160        170 
TARLFERIIE EEQAHLTYYE NIGSHIKNLG DTYLAKIAGT PSSTGTASKG FVTATPAAE 

« Hide

References

« Hide 'large scale' references
[1]"The genetic organization of Desulfovibrio desulphuricans ATCC 27774 bacterioferritin and rubredoxin-2 genes: involvement of rubredoxin in iron metabolism."
da Costa P.N., Romao C.V., LeGall J., Xavier A.V., Melo E., Teixeira M., Saraiva L.M.
Mol. Microbiol. 41:217-227(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Hazen T.C.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27774 / DSM 6949.
[3]"A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans ATCC 27774."
Romao C.V., Regalla M., Xavier A.V., Teixeira M., Liu M.-Y., Le Gall J.
Biochemistry 39:6841-6849(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, SUBUNIT, REDOX POTENTIOMETRY OF HEME, ABSORPTION SPECTROSCOPY, EPR SPECTROSCOPY.
[4]"Iron-coproporphyrin III is a natural cofactor in bacterioferritin from the anaerobic bacterium Desulfovibrio desulfuricans."
Romao C.V., Louro R., Timkovich R., Lubben M., Liu M.Y., LeGall J., Xavier A.V., Teixeira M.
FEBS Lett. 480:213-216(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[5]"Structure determination of bacterioferritin from Desulfovibrio desulfuricans by the MAD method at the Fe K-edge."
Coelho A.V., Macedo S., Matias P.M., Thompson A.W., LeGall J., Carrondo M.A.
Acta Crystallogr. D 57:326-329(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[6]"The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans."
Macedo S., Romao C.V., Mitchell E., Matias P.M., Liu M.Y., Xavier A.V., LeGall J., Teixeira M., Lindley P., Carrondo M.A.
Nat. Struct. Biol. 10:285-290(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF321851 Genomic DNA. Translation: AAK60120.1.
CP001358 Genomic DNA. Translation: ACL49289.1.
RefSeqYP_002479967.1. NC_011883.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NF4X-ray2.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
1NF6X-ray2.35A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
1NFVX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
ProteinModelPortalQ93PP9.
SMRQ93PP9. Positions 2-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING525146.Ddes_1387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL49289; ACL49289; Ddes_1387.
GeneID7285082.
KEGGdds:Ddes_1387.
PATRIC21736512. VBIDesDes50650_1607.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2193.
HOGENOMHOG000262383.
KOK03594.
OrthoDBEOG6WDSKP.

Enzyme and pathway databases

BioCycDDES525146:GIWF-1431-MONOMER.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFPIRSF002560. Bacterioferritin. 1 hit.
PRINTSPR00601. BACFERRITIN.
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ93PP9.

Entry information

Entry nameBFR_DESDA
AccessionPrimary (citable) accession number: Q93PP9
Secondary accession number(s): B8J0L2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references