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Q93PP9

- BFR_DESDA

UniProt

Q93PP9 - BFR_DESDA

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Protein
Bacterioferritin
Gene
bfr, Ddes_1387
Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Status
Reviewed - 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

Binds 1 Fe-coproporphyrin III group per dimer.1 Publication
Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Iron 11 Publication
Metal bindingi56 – 561Iron 11 Publication
Metal bindingi56 – 561Iron 21 Publication
Metal bindingi57 – 571Iron (Fe-coproporphyrin III axial ligand); shared with dimeric partner1 Publication
Metal bindingi59 – 591Iron 11 Publication
Metal bindingi99 – 991Iron 21 Publication
Metal bindingi132 – 1321Iron 11 Publication
Metal bindingi132 – 1321Iron 21 Publication
Metal bindingi135 – 1351Iron 21 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. intracellular sequestering of iron ion Source: UniProtKB
  2. 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.

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: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 179179Bacterioferritin
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ93PP9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 150150Ferritin-like diiron
Add
BLAST

Sequence similaritiesi

Belongs to the bacterioferritin family.

Phylogenomic databases

eggNOGiCOG2193.
HOGENOMiHOG000262383.
KOiK03594.
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

MAGNREDRKA KVIEVLNKAR AMELHAIHQY MNQHYSLDDM DYGELAANMK    50
LIAIDEMRHA ENFAERIKEL GGEPTTQKEG KVVTGQAVPV IYESDADQED 100
ATIEAYSQFL KVCKEQGDIV TARLFERIIE EEQAHLTYYE NIGSHIKNLG 150
DTYLAKIAGT PSSTGTASKG FVTATPAAE 179
Length:179
Mass (Da):19,881
Last modified:December 1, 2001 - v1
Checksum:i09E3387462FED3A3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi7285082.
KEGGidds:Ddes_1387.
PATRICi21736512. VBIDesDes50650_1607.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF321851 Genomic DNA. Translation: AAK60120.1 .
CP001358 Genomic DNA. Translation: ACL49289.1 .
RefSeqi WP_012625013.1. NC_011883.1.
YP_002479967.1. NC_011883.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NF4 X-ray 2.05 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-179 [» ]
1NF6 X-ray 2.35 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-179 [» ]
1NFV X-ray 1.95 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-179 [» ]
ProteinModelPortali Q93PP9.
SMRi Q93PP9. Positions 2-172.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 525146.Ddes_1387.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL49289 ; ACL49289 ; Ddes_1387 .
GeneIDi 7285082.
KEGGi dds:Ddes_1387.
PATRICi 21736512. VBIDesDes50650_1607.

Phylogenomic databases

eggNOGi COG2193.
HOGENOMi HOG000262383.
KOi K03594.
OrthoDBi EOG6WDSKP.

Enzyme and pathway databases

BioCyci DDES525146:GIWF-1431-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q93PP9.

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.
PROSITEi PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 77 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

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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