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Protein

Bacterioferritin

Gene

bfr

Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Iron 1
Metal bindingi56 – 561Iron 1
Metal bindingi56 – 561Iron 2
Metal bindingi57 – 571Iron (Fe-coproporphyrin III axial ligand); shared with dimeric partner
Metal bindingi59 – 591Iron 1
Metal bindingi99 – 991Iron 2
Metal bindingi132 – 1321Iron 1
Metal bindingi132 – 1321Iron 2
Metal bindingi135 – 1351Iron 2

GO - Molecular functioni

GO - Biological processi

  • intracellular sequestering of iron ion Source: UniProtKB
  • iron ion transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciDDES525146:GIWF-1431-MONOMER.
BRENDAi1.16.3.1. 1905.

Names & Taxonomyi

Protein namesi
Recommended name:
Bacterioferritin (EC:1.16.3.1)
Short name:
BFR
Gene namesi
Name:bfr
Ordered Locus Names:Ddes_1387
OrganismiDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Taxonomic identifieri525146 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000002598 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  • cell Source: GOC
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 179179BacterioferritinPRO_0000192591Add
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.1 Publication

Protein-protein interaction databases

STRINGi525146.Ddes_1387.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3935Combined sources
Helixi43 – 6927Combined sources
Helixi88 – 11528Combined sources
Helixi119 – 14931Combined sources
Helixi151 – 1577Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NF4X-ray2.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
1NF6X-ray2.35A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
1NFVX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
ProteinModelPortaliQ93PP9.
SMRiQ93PP9. Positions 2-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ93PP9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 150150Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2193.
HOGENOMiHOG000262383.
KOiK03594.
OMAiTIIEEEQ.
OrthoDBiEOG6WDSKP.

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.
PROSITEiPS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93PP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGNREDRKA KVIEVLNKAR AMELHAIHQY MNQHYSLDDM DYGELAANMK
60 70 80 90 100
LIAIDEMRHA ENFAERIKEL GGEPTTQKEG KVVTGQAVPV IYESDADQED
110 120 130 140 150
ATIEAYSQFL KVCKEQGDIV TARLFERIIE EEQAHLTYYE NIGSHIKNLG
160 170
DTYLAKIAGT PSSTGTASKG FVTATPAAE
Length:179
Mass (Da):19,881
Last modified:December 1, 2001 - v1
Checksum:i09E3387462FED3A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321851 Genomic DNA. Translation: AAK60120.1.
CP001358 Genomic DNA. Translation: ACL49289.1.
RefSeqiWP_012625013.1. NC_011883.1.
YP_002479967.1. NC_011883.1.

Genome annotation databases

EnsemblBacteriaiACL49289; ACL49289; Ddes_1387.
KEGGidds:Ddes_1387.
PATRICi21736512. VBIDesDes50650_1607.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321851 Genomic DNA. Translation: AAK60120.1.
CP001358 Genomic DNA. Translation: ACL49289.1.
RefSeqiWP_012625013.1. NC_011883.1.
YP_002479967.1. NC_011883.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NF4X-ray2.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
1NF6X-ray2.35A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
1NFVX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-179[»]
ProteinModelPortaliQ93PP9.
SMRiQ93PP9. Positions 2-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi525146.Ddes_1387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL49289; ACL49289; Ddes_1387.
KEGGidds:Ddes_1387.
PATRICi21736512. VBIDesDes50650_1607.

Phylogenomic databases

eggNOGiCOG2193.
HOGENOMiHOG000262383.
KOiK03594.
OMAiTIIEEEQ.
OrthoDBiEOG6WDSKP.

Enzyme and pathway databases

BioCyciDDES525146:GIWF-1431-MONOMER.
BRENDAi1.16.3.1. 1905.

Miscellaneous databases

EvolutionaryTraceiQ93PP9.

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.
PROSITEiPS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genetic organization of Desulfovibrio desulphuricans ATCC 27774 bacterioferritin and rubredoxin-2 genes: involvement of rubredoxin in iron metabolism."
    da Costa P.N., Romao C.V., LeGall J., Xavier A.V., Melo E., Teixeira M., Saraiva L.M.
    Mol. Microbiol. 41:217-227(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.
    , Kyrpides N., Ovchinnikova G., Hazen T.C.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27774 / DSM 6949.
  3. "A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans ATCC 27774."
    Romao C.V., Regalla M., Xavier A.V., Teixeira M., Liu M.-Y., Le Gall J.
    Biochemistry 39:6841-6849(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, SUBUNIT, REDOX POTENTIOMETRY OF HEME, ABSORPTION SPECTROSCOPY, EPR SPECTROSCOPY.
  4. "Iron-coproporphyrin III is a natural cofactor in bacterioferritin from the anaerobic bacterium Desulfovibrio desulfuricans."
    Romao C.V., Louro R., Timkovich R., Lubben M., Liu M.Y., LeGall J., Xavier A.V., Teixeira M.
    FEBS Lett. 480:213-216(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  5. "Structure determination of bacterioferritin from Desulfovibrio desulfuricans by the MAD method at the Fe K-edge."
    Coelho A.V., Macedo S., Matias P.M., Thompson A.W., LeGall J., Carrondo M.A.
    Acta Crystallogr. D 57:326-329(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  6. "The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans."
    Macedo S., Romao C.V., Mitchell E., Matias P.M., Liu M.Y., Xavier A.V., LeGall J., Teixeira M., Lindley P., Carrondo M.A.
    Nat. Struct. Biol. 10:285-290(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).

Entry informationi

Entry nameiBFR_DESDA
AccessioniPrimary (citable) accession number: Q93PP9
Secondary accession number(s): B8J0L2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 83 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, Complete proteome, Direct protein sequencing, Reference proteome

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.