Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bacterioferritin

Gene

bfr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.2 Publications

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • heme b1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.1 Publication
  • Fe cation1 PublicationNote: Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center. In BFR, the ferroxidase center appears to function as a true di-iron catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins.1 Publication

Enzyme regulationi

Iron oxidation is inhibited by Zn2+, which binds at the ferroxidase center with a higher affinity that Fe2+. The occupation of the ferroxidase center by Zn2+ also severely restricts the ability of BFR to form an iron core.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi18Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi46Iron 3PROSITE-ProRule annotation1 Publication1
Metal bindingi50Iron 3PROSITE-ProRule annotation1 Publication1
Metal bindingi51Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi51Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi52Iron (heme axial ligand); shared with dimeric partnerPROSITE-ProRule annotation1 Publication1
Metal bindingi54Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi94Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi127Iron 1PROSITE-ProRule annotation1 Publication1
Metal bindingi127Iron 2PROSITE-ProRule annotation1 Publication1
Metal bindingi130Iron 2PROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • ferric iron binding Source: InterPro
  • ferroxidase activity Source: Reactome
  • heme binding Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • iron ion binding Source: EcoCyc
  • oxidoreductase activity Source: EcoliWiki

GO - Biological processi

  • intracellular sequestering of iron ion Source: EcoCyc
  • iron ion transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10113-MONOMER.
ECOL316407:JW3298-MONOMER.
MetaCyc:EG10113-MONOMER.
BRENDAi1.16.3.1. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Bacterioferritin (EC:1.16.3.1)
Short name:
BFR
Alternative name(s):
Cytochrome b-1
Cytochrome b-557
Gene namesi
Name:bfr
Ordered Locus Names:b3336, JW3298
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10113. bfr.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi18E → A: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication1
Mutagenesisi31M → H or L: No loss of heme binding. 1 Publication1
Mutagenesisi46H → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication1
Mutagenesisi50D → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication1
Mutagenesisi52M → H or L: Loss of heme binding. Is still capable of accumulating iron. 1 Publication1
Mutagenesisi86M → L: No loss of heme binding. 1 Publication1
Mutagenesisi127E → Q: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core. 1 Publication1
Mutagenesisi130H → E: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001925921 – 158BacterioferritinAdd BLAST158

Proteomic databases

EPDiP0ABD3.
PaxDbiP0ABD3.
PRIDEiP0ABD3.

Interactioni

Subunit structurei

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 as a ferric-oxy-hydroxide mineral core.7 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262466. 15 interactors.
DIPiDIP-36167N.
IntActiP0ABD3. 2 interactors.
STRINGi511145.b3336.

Structurei

Secondary structure

1158
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 34Combined sources30
Helixi38 – 64Combined sources27
Helixi83 – 110Combined sources28
Helixi114 – 144Combined sources31
Helixi146 – 152Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCFX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
1BFRX-ray2.94A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
2HTNX-ray2.50A/B/C/D/E/F/G/H1-158[»]
2VXIX-ray1.91A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
2Y3QX-ray1.55A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1JX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1LX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1MX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1NX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1OX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1PX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1QX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E2CX-ray1.80A/B1-158[»]
3GHQX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4CVPX-ray2.11A1-158[»]
4CVRX-ray1.10A1-158[»]
4CVSX-ray1.39A1-158[»]
4CVTX-ray1.79A1-158[»]
4U3GX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4XKSX-ray1.57A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4XKTX-ray1.82A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4XKUX-ray1.78A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
ProteinModelPortaliP0ABD3.
SMRiP0ABD3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABD3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 145Ferritin-like diironPROSITE-ProRule annotationAdd BLAST145

Sequence similaritiesi

Belongs to the bacterioferritin family.Curated
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108UQY. Bacteria.
COG2193. LUCA.
HOGENOMiHOG000262383.
InParanoidiP0ABD3.
KOiK03594.
OMAiEMKHADQ.
PhylomeDBiP0ABD3.

Family and domain databases

CDDicd00907. Bacterioferritin. 1 hit.
Gene3Di1.20.1260.10. 1 hit.
InterProiIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFiPIRSF002560. Bacterioferritin. 1 hit.
PRINTSiPR00601. BACFERRITIN.
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR00754. bfr. 1 hit.
PROSITEiPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABD3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID
60 70 80 90 100
EMKHADRYIE RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN
110 120 130 140 150
LREAIGYADS VHDYVSRDMM IEILRDEEGH IDWLETELDL IQKMGLQNYL

QAQIREEG
Length:158
Mass (Da):18,495
Last modified:October 25, 2005 - v1
Checksum:iA6C86CE1CD8F865A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53K → M AA sequence (PubMed:2644932).Curated1

Mass spectrometryi

Molecular mass is 18496±2 Da from positions 1 - 158. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti5 – 7TKV → VKI in strain: ECOR 30. 3
Natural varianti38K → M in strain: ECOR 30. 1
Natural varianti57R → K in strain: ECOR 30. 1
Natural varianti68L → I in strain: ECOR 30. 1
Natural varianti78N → G in strain: ECOR 30. 1
Natural varianti88R → Q in strain: ECOR 30. 1
Natural varianti92A → R in strain: ECOR 30. 1
Natural varianti96D → E in strain: ECOR 30. 1
Natural varianti100N → D in strain: ECOR 30. 1
Natural varianti106G → A in strain: ECOR 30. 1
Natural varianti125R → A in strain: ECOR 30. 1
Natural varianti142 – 144QKM → GKI in strain: ECOR 30. 3
Natural varianti152 – 158AQIREEG → SQIKVKD in strain: ECOR 30. 7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27176 mRNA. Translation: AAC13987.1.
AF058450 Genomic DNA. Translation: AAC14288.1.
U18997 Genomic DNA. Translation: AAA58133.1.
U00096 Genomic DNA. Translation: AAC76361.1.
AP009048 Genomic DNA. Translation: BAE77955.1.
L28106 Genomic DNA. Translation: AAC36929.1.
PIRiJV0032. FREC.
RefSeqiNP_417795.1. NC_000913.3.
WP_000675504.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76361; AAC76361; b3336.
BAE77955; BAE77955; BAE77955.
GeneIDi947839.
KEGGiecj:JW3298.
eco:b3336.
PATRICi32122104. VBIEscCol129921_3429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27176 mRNA. Translation: AAC13987.1.
AF058450 Genomic DNA. Translation: AAC14288.1.
U18997 Genomic DNA. Translation: AAA58133.1.
U00096 Genomic DNA. Translation: AAC76361.1.
AP009048 Genomic DNA. Translation: BAE77955.1.
L28106 Genomic DNA. Translation: AAC36929.1.
PIRiJV0032. FREC.
RefSeqiNP_417795.1. NC_000913.3.
WP_000675504.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCFX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
1BFRX-ray2.94A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
2HTNX-ray2.50A/B/C/D/E/F/G/H1-158[»]
2VXIX-ray1.91A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
2Y3QX-ray1.55A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1JX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1LX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1MX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1NX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1OX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1PX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1QX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E2CX-ray1.80A/B1-158[»]
3GHQX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4CVPX-ray2.11A1-158[»]
4CVRX-ray1.10A1-158[»]
4CVSX-ray1.39A1-158[»]
4CVTX-ray1.79A1-158[»]
4U3GX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4XKSX-ray1.57A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4XKTX-ray1.82A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
4XKUX-ray1.78A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
ProteinModelPortaliP0ABD3.
SMRiP0ABD3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262466. 15 interactors.
DIPiDIP-36167N.
IntActiP0ABD3. 2 interactors.
STRINGi511145.b3336.

Proteomic databases

EPDiP0ABD3.
PaxDbiP0ABD3.
PRIDEiP0ABD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76361; AAC76361; b3336.
BAE77955; BAE77955; BAE77955.
GeneIDi947839.
KEGGiecj:JW3298.
eco:b3336.
PATRICi32122104. VBIEscCol129921_3429.

Organism-specific databases

EchoBASEiEB0111.
EcoGeneiEG10113. bfr.

Phylogenomic databases

eggNOGiENOG4108UQY. Bacteria.
COG2193. LUCA.
HOGENOMiHOG000262383.
InParanoidiP0ABD3.
KOiK03594.
OMAiEMKHADQ.
PhylomeDBiP0ABD3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10113-MONOMER.
ECOL316407:JW3298-MONOMER.
MetaCyc:EG10113-MONOMER.
BRENDAi1.16.3.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP0ABD3.
PROiP0ABD3.

Family and domain databases

CDDicd00907. Bacterioferritin. 1 hit.
Gene3Di1.20.1260.10. 1 hit.
InterProiIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFiPIRSF002560. Bacterioferritin. 1 hit.
PRINTSiPR00601. BACFERRITIN.
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR00754. bfr. 1 hit.
PROSITEiPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBFR_ECOLI
AccessioniPrimary (citable) accession number: P0ABD3
Secondary accession number(s): O68931, P11056, Q2M701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe2+ binding and oxidation at the ferroxidase center.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.