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Q59738

- BFR_RHOCA

UniProt

Q59738 - BFR_RHOCA

Protein

Bacterioferritin

Gene

bfr

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    GO - Biological processi

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

    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 – 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.
    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

    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...
    MobiDBi 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: October 1, 2014
    This is version 75 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