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O50171 (BFR1_MAGMG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 subunit 1

Short name=BFR 1
EC=1.16.3.1
Gene names
Name:bfr1
OrganismMagnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)
Taxonomic identifier188 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 Potential.

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

Subunit structure

Oligomer 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 By similarity.

Sequence similarities

Belongs to the bacterioferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
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 – 164164Bacterioferritin subunit 1
PRO_0000192596

Regions

Domain1 – 147147Ferritin-like diiron

Sites

Metal binding181Iron 1 By similarity
Metal binding491Iron (heme axial ligand); shared with dimeric partner Potential
Metal binding511Iron 1 By similarity
Metal binding511Iron 2 By similarity
Metal binding541Iron 1 By similarity
Metal binding941Iron 2 By similarity
Metal binding1291Iron 1 By similarity
Metal binding1291Iron 2 By similarity
Metal binding1321Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O50171 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 6B837DCAFCD72358

FASTA16418,491
        10         20         30         40         50         60 
MKGKKSVISR LNKLLVGELV AADQYFVHSR MYQEWGLQKL YERIDHERMD ELEHADLLIR 

        70         80         90        100        110        120 
RILFLEGTPD ISKRPGPNIG KDVPSMLKND LDYELAVIAE LKEVIAHCEG PKRTMTAAAS 

       130        140        150        160 
CSTILEETEQ DHTLWLEQQL GLIARMGLQN YIQSAAGDIA QGAS 

« Hide

References

[1]"Evidence for two types of subunits in the bacterioferritin of Magnetospirillum magnetotacticum."
Bertani L.E., Huang J.S., Weir B.A., Kirschvink J.L.
Gene 201:31-36(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MS-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF001959 Genomic DNA. Translation: AAC91253.1.

3D structure databases

ProteinModelPortalO50171.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameBFR1_MAGMG
AccessionPrimary (citable) accession number: O50171
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: October 16, 2013
This is version 67 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