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Q59738 (BFR_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. 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
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length161 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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer.

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

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.

Sequence similarities

Belongs to the bacterioferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Bacterioferritin
PRO_0000192611

Regions

Domain1 – 145145Ferritin-like diiron

Sites

Metal binding181Iron 1
Metal binding511Iron 1
Metal binding511Iron 2
Metal binding521Iron (heme axial ligand); shared with dimeric partner
Metal binding541Iron 1
Metal binding941Iron 2
Metal binding1271Iron 1
Metal binding1271Iron 2
Metal binding1301Iron 2

Secondary structure

........... 161
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59738 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 9E534CBC531EC709

FASTA16118,173
        10         20         30         40         50         60 
MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE EMGHADKIIA 

        70         80         90        100        110        120 
RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL YREARDYCAE VGDIVSKNIF 

       130        140        150        160 
ESLITDEEGH VDFLETQISL YDRLGPQGFA LLNAAPMDAA E 

« Hide

References

[1]"Isolation, characterisation and expression of the bacterioferritin gene of Rhodobacter capsulatus."
Penfold C.N., Ringeling P.L., Davy S.L., Moore G.R., McEwan A.G., Spiro S.
FEMS Microbiol. Lett. 139:143-148(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 938 / 37b4.
[2]"The 2.6 A resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position'."
Cobessi D., Huang L.-S., Ban M., Pon N.G., Daldal F., Berry E.A.
Acta Crystallogr. D 58:29-38(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z54247 Genomic DNA. Translation: CAA91017.1.
PIRS48182.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGCX-ray2.60A/B/C1-161[»]
ProteinModelPortalQ59738.
SMRQ59738. Positions 1-160.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000262383.

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.
TIGRFAMsTIGR00754. bfr. 1 hit.
PROSITEPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ59738.

Entry information

Entry nameBFR_RHOCA
AccessionPrimary (citable) accession number: Q59738
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 74 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