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Protein

Bacterioferritin

Gene

bfr

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.By similarity
  • Fe cationBy similarityNote: Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Iron 1PROSITE-ProRule annotation
Metal bindingi51 – 511Iron 1PROSITE-ProRule annotation
Metal bindingi51 – 511Iron 2PROSITE-ProRule annotation
Metal bindingi52 – 521Iron (heme axial ligand); shared with dimeric partnerPROSITE-ProRule annotation
Metal bindingi54 – 541Iron 1PROSITE-ProRule annotation
Metal bindingi94 – 941Iron 2PROSITE-ProRule annotation
Metal bindingi127 – 1271Iron 1PROSITE-ProRule annotation
Metal bindingi127 – 1271Iron 2PROSITE-ProRule annotation
Metal bindingi130 – 1301Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bacterioferritin (EC:1.16.3.1)
Short name:
BFR
Alternative name(s):
Cytochrome b-557.5
Gene namesi
Name:bfr
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156BacterioferritinPRO_0000192588Add
BLAST

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.By similarity

Protein-protein interaction databases

STRINGi322710.Avin_14050.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3430Combined sources
Helixi38 – 6427Combined sources
Helixi83 – 11028Combined sources
Helixi114 – 14431Combined sources
Helixi146 – 1516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP22759.
SMRiP22759. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 145145Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

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.

P22759-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGDKIVIQH LNKILGNELI AINQYFLHAR MYEDWGLEKL GKHEYHESID
60 70 80 90 100
EMKHADKLIK RILFLEGLPN LQELGKLLIG EHTKEMLECD LKLEQAGLPD
110 120 130 140 150
LKAAIAYCES VGDYASRELL EDILESEEDH IDWLETQLDL IDKIGLENYL

QSQMDE
Length:156
Mass (Da):18,105
Last modified:May 1, 1992 - v2
Checksum:i468C2F059240A647
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83692 Genomic DNA. Translation: AAA22121.1.
PIRiA41983.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83692 Genomic DNA. Translation: AAA22121.1.
PIRiA41983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP22759.
SMRiP22759. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_14050.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP22759.

Family and domain databases

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...

Publicationsi

  1. 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.

Entry informationi

Entry nameiBFR_AZOVI
AccessioniPrimary (citable) accession number: P22759
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.