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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Iron 1
Metal bindingi51 – 511Iron 1
Metal bindingi51 – 511Iron 2
Metal bindingi52 – 521Iron (heme axial ligand); shared with dimeric partner
Metal bindingi54 – 541Iron 1
Metal bindingi94 – 941Iron 2
Metal bindingi127 – 1271Iron 1
Metal bindingi127 – 1271Iron 2
Metal bindingi130 – 1301Iron 2

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
  2. iron ion transport Source: InterPro
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161BacterioferritinPRO_0000192611Add
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.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3430Combined sources
Helixi38 – 6427Combined sources
Helixi83 – 11129Combined sources
Helixi114 – 14431Combined sources
Helixi146 – 1527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGCX-ray2.60A/B/C1-161[»]
ProteinModelPortaliQ59738.
SMRiQ59738. Positions 1-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59738.

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

Phylogenomic databases

HOGENOMiHOG000262383.

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGCX-ray2.60A/B/C1-161[»]
ProteinModelPortaliQ59738.
SMRiQ59738. Positions 1-160.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000262383.

Miscellaneous databases

EvolutionaryTraceiQ59738.

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. "Isolation, characterisation and expression of the bacterioferritin gene of Rhodobacter capsulatus."
    Penfold C.N., Ringeling P.L., Davy S.L., Moore G.R., McEwan A.G., Spiro S.
    FEMS Microbiol. Lett. 139:143-148(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 938 / 37b4.
  2. "The 2.6 A resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position'."
    Cobessi D., Huang L.-S., Ban M., Pon N.G., Daldal F., Berry E.A.
    Acta Crystallogr. D 58:29-38(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

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 26, 2014
This is version 76 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

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.