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P22759

- BFR_AZOVI

UniProt

P22759 - BFR_AZOVI

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Protein
Bacterioferritin
Gene
bfr
Organism
Azotobacter vinelandii
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 By similarity.
Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center By similarity.

Sites

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

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
Alternative name(s):
Cytochrome b-557.5
Gene namesi
Name:bfr
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Bacterioferritin
PRO_0000192588Add
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 By similarity.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3430
Helixi38 – 6427
Helixi83 – 11028
Helixi114 – 14431
Helixi146 – 1516

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SOFX-ray2.60A/B/C/D/E/F/G/H1-156[»]
2FKZX-ray2.00A/B/C/D/E/F/G/H1-155[»]
2FL0X-ray2.70A/B/C/D/E/F/G/H1-155[»]
ProteinModelPortaliP22759.
SMRiP22759. Positions 1-155.

Miscellaneous databases

EvolutionaryTraceiP22759.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the bacterioferritin family.

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.

P22759-1 [UniParc]FASTAAdd to Basket

« Hide

MKGDKIVIQH LNKILGNELI AINQYFLHAR MYEDWGLEKL GKHEYHESID    50
EMKHADKLIK RILFLEGLPN LQELGKLLIG EHTKEMLECD LKLEQAGLPD 100
LKAAIAYCES VGDYASRELL EDILESEEDH IDWLETQLDL IDKIGLENYL 150
QSQMDE 156
Length:156
Mass (Da):18,105
Last modified:May 1, 1992 - v2
Checksum:i468C2F059240A647
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83692 Genomic DNA. Translation: AAA22121.1.
PIRiA41983.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83692 Genomic DNA. Translation: AAA22121.1 .
PIRi A41983.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SOF X-ray 2.60 A/B/C/D/E/F/G/H 1-156 [» ]
2FKZ X-ray 2.00 A/B/C/D/E/F/G/H 1-155 [» ]
2FL0 X-ray 2.70 A/B/C/D/E/F/G/H 1-155 [» ]
ProteinModelPortali P22759.
SMRi P22759. Positions 1-155.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P22759.

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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Physical, chemical and immunological properties of the bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vinelandii."
    Andrews S.C., Findlay J.B.C., Guest J.R., Harrison P.M., Keen J.N., Smith J.M.A.
    Biochim. Biophys. Acta 1078:111-116(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-70.

Entry informationi

Entry nameiBFR_AZOVI
AccessioniPrimary (citable) accession number: P22759
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 1, 1992
Last modified: October 16, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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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