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Protein

Bacterioferritin

Gene

bfr

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
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 bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
  • Fe cationNote: Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi18Iron 11
Metal bindingi51Iron 11
Metal bindingi51Iron 21
Metal bindingi52Iron (heme axial ligand); shared with dimeric partner1
Metal bindingi54Iron 11
Metal bindingi94Iron 21
Metal bindingi127Iron 11
Metal bindingi127Iron 21
Metal bindingi130Iron 21

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
Gene namesi
Name:bfr
OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifieri1061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001926111 – 161BacterioferritinAdd BLAST161

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.

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00913.

Structurei

Secondary structure

1161
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 34Combined sources30
Helixi38 – 64Combined sources27
Helixi83 – 111Combined sources29
Helixi114 – 144Combined sources31
Helixi146 – 152Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JGCX-ray2.60A/B/C1-161[»]
ProteinModelPortaliQ59738.
SMRiQ59738.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59738.

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.

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.

Q59738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE
60 70 80 90 100
EMGHADKIIA RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL
110 120 130 140 150
YREARDYCAE VGDIVSKNIF ESLITDEEGH VDFLETQISL YDRLGPQGFA
160
LLNAAPMDAA E
Length:161
Mass (Da):18,173
Last modified:November 1, 1997 - v1
Checksum:i9E534CBC531EC709
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54247 Genomic DNA. Translation: CAA91017.1.
PIRiS48182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54247 Genomic DNA. Translation: CAA91017.1.
PIRiS48182.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JGCX-ray2.60A/B/C1-161[»]
ProteinModelPortaliQ59738.
SMRiQ59738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108UQY. Bacteria.
COG2193. LUCA.
HOGENOMiHOG000262383.

Miscellaneous databases

EvolutionaryTraceiQ59738.

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_RHOCA
AccessioniPrimary (citable) accession number: Q59738
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.