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Q59738

- BFR_RHOCA

UniProt

Q59738 - BFR_RHOCA

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Protein
Bacterioferritin
Gene
bfr
Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed - 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

Binds 1 heme B (iron-protoporphyrin IX) group per dimer.
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
Complete GO annotation...

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 – 161161Bacterioferritin
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGCX-ray2.60A/B/C1-161[»]
ProteinModelPortaliQ59738.
SMRiQ59738. Positions 1-160.

Miscellaneous databases

EvolutionaryTraceiQ59738.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 145145Ferritin-like diiron
Add
BLAST

Sequence similaritiesi

Belongs to the bacterioferritin family.

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

MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE    50
EMGHADKIIA RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL 100
YREARDYCAE VGDIVSKNIF ESLITDEEGH VDFLETQISL YDRLGPQGFA 150
LLNAAPMDAA E 161
Length:161
Mass (Da):18,173
Last modified:November 1, 1997 - v1
Checksum:i9E534CBC531EC709
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54247 Genomic DNA. Translation: CAA91017.1.
PIRiS48182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54247 Genomic DNA. Translation: CAA91017.1 .
PIRi S48182.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JGC X-ray 2.60 A/B/C 1-161 [» ]
ProteinModelPortali Q59738.
SMRi Q59738. Positions 1-160.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000262383.

Miscellaneous databases

EvolutionaryTracei Q59738.

Family and domain databases

Gene3Di 1.20.1260.10. 1 hit.
InterProi IPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view ]
Pfami PF00210. Ferritin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002560. Bacterioferritin. 1 hit.
PRINTSi PR00601. BACFERRITIN.
SUPFAMi SSF47240. SSF47240. 1 hit.
TIGRFAMsi TIGR00754. bfr. 1 hit.
PROSITEi PS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 74 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

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