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Protein

Bacterioferritin

Gene

bfr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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.

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: EcoCyc
  • 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

Keywordsi

Molecular functionOxidoreductase
Biological processIron storage
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10113-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: EcoCyc
  • membrane Source: UniProtKB

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-907496,EBI-907496

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262466, 23 interactors
DIPiDIP-36167N
IntActiP0ABD3, 3 interactors
STRINGi316385.ECDH10B_3511

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[»]
5XGOX-ray1.99A/B/C/D/E/F/G/H/I/J/K/L138-158[»]
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

Phylogenomic databases

eggNOGiENOG4108UQY Bacteria
COG2193 LUCA
HOGENOMiHOG000262383
InParanoidiP0ABD3
KOiK03594
OMAiTPEMLKC
PhylomeDBiP0ABD3

Family and domain databases

CDDicd00907 Bacterioferritin, 1 hit
Gene3Di1.20.1260.10, 1 hit
InterProiView protein in InterPro
IPR002024 Bacterioferritin
IPR012347 Ferritin-like
IPR009040 Ferritin-like_diiron
IPR009078 Ferritin-like_SF
IPR008331 Ferritin_DPS_dom
PfamiView protein in Pfam
PF00210 Ferritin, 1 hit
PIRSFiPIRSF002560 Bacterioferritin, 1 hit
PRINTSiPR00601 BACFERRITIN
SUPFAMiSSF47240 SSF47240, 1 hit
TIGRFAMsiTIGR00754 bfr, 1 hit
PROSITEiView protein in PROSITE
PS00549 BACTERIOFERRITIN, 1 hit
PS50905 FERRITIN_LIKE, 1 hit

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
PATRICifig|1411691.4.peg.3395

Similar proteinsi

Entry informationi

Entry nameiBFR_ECOLI
AccessioniPrimary (citable) accession number: P0ABD3
Secondary accession number(s): O68931, P11056, Q2M701
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: April 25, 2018
This is version 103 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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