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P22759 (BFR_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 84. 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
Alternative name(s):
Cytochrome b-557.5
Gene names
Name:bfr
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length156 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 By similarity.

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

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 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
   Technical term3D-structure
Direct protein sequencing
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 – 156156Bacterioferritin
PRO_0000192588

Regions

Domain1 – 145145Ferritin-like diiron

Sites

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

Secondary structure

........... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22759 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 468C2F059240A647

FASTA15618,105
        10         20         30         40         50         60 
MKGDKIVIQH LNKILGNELI AINQYFLHAR MYEDWGLEKL GKHEYHESID EMKHADKLIK 

        70         80         90        100        110        120 
RILFLEGLPN LQELGKLLIG EHTKEMLECD LKLEQAGLPD LKAAIAYCES VGDYASRELL 

       130        140        150 
EDILESEEDH IDWLETQLDL IDKIGLENYL QSQMDE 

« Hide

References

[1]"Unification of the ferritin family of proteins."
Grossman M.J., Hinton S.M., Minak-Bernero V., Slaughter C., Stiefel E.I.
Proc. Natl. Acad. Sci. U.S.A. 89:2419-2423(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Physical, chemical and immunological properties of the bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vinelandii."
Andrews S.C., Findlay J.B.C., Guest J.R., Harrison P.M., Keen J.N., Smith J.M.A.
Biochim. Biophys. Acta 1078:111-116(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83692 Genomic DNA. Translation: AAA22121.1.
PIRA41983.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SOFX-ray2.60A/B/C/D/E/F/G/H1-156[»]
2FKZX-ray2.00A/B/C/D/E/F/G/H1-155[»]
2FL0X-ray2.70A/B/C/D/E/F/G/H1-155[»]
ProteinModelPortalP22759.
SMRP22759. Positions 1-155.
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...

Other

EvolutionaryTraceP22759.

Entry information

Entry nameBFR_AZOVI
AccessionPrimary (citable) accession number: P22759
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 1, 1992
Last modified: October 16, 2013
This is version 84 of the entry and version 2 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