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P24602 (BFR_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bacterioferritin

Short name=BFR
EC=1.16.3.1
Gene names
Name:bfr
Ordered Locus Names:sll1341
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer Potential.

Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center By similarity.

Subunit structure

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.

Sequence similarities

Belongs to the bacterioferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156Bacterioferritin
PRO_0000192613

Regions

Domain1 – 146146Ferritin-like diiron

Sites

Metal binding181Iron 1 By similarity
Metal binding481Iron (heme axial ligand); shared with dimeric partner Potential
Metal binding511Iron 1 By similarity
Metal binding511Iron 2 By similarity
Metal binding541Iron 1 By similarity
Metal binding941Iron 2 By similarity
Metal binding1281Iron 1 By similarity
Metal binding1281Iron 2 By similarity
Metal binding1311Iron 2 By similarity

Experimental info

Sequence conflict53 – 542AH → HA AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24602 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 7C1A13B31157AF86

FASTA15618,331
        10         20         30         40         50         60 
MKGKPAVLAQ LHKLLRGELA ARDQYFIHSR MYQDWGLEKL YSRIDHEMQD ETAHASLLIE 

        70         80         90        100        110        120 
RILFLEETPD LSQQDPIRVG KTVPEMLQYD LDYEYEVIAN LKEAMAVCEQ EQDYQSRDLL 

       130        140        150 
LKILADTEED HAYWLEKQLG LIEKIGLQNY LQSQMS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.
[2]"Purification, characterization and function of bacterioferritin from the cyanobacterium Synechocystis P.C.C. 6803."
Laulhere J.-P., Laboure A.-M., van Wuytswinkel O., Gagnon J., Briat J.-F.
Biochem. J. 281:785-793(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-54.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA18637.1.
PIRS76725.
RefSeqNP_442825.1. NC_000911.1.
YP_005652886.1. NC_017277.1.
YP_007452701.1. NC_020286.1.

3D structure databases

ProteinModelPortalP24602.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1148.sll1341.

Proteomic databases

PaxDbP24602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18637; BAA18637; BAA18637.
GeneID12255164.
14618385.
952063.
KEGGsyn:sll1341.
syy:SYNGTS_2933.
syz:MYO_129610.
PATRIC23843424. VBISynSp132158_3248.

Phylogenomic databases

eggNOGCOG2193.
HOGENOMHOG000262383.
KOK03594.
OMADWGLNEL.
OrthoDBEOG6WDSKP.
PhylomeDBP24602.
ProtClustDBCLSK2301948.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFPIRSF002560. Bacterioferritin. 1 hit.
PRINTSPR00601. BACFERRITIN.
SUPFAMSSF47240. SSF47240. 1 hit.
TIGRFAMsTIGR00754. bfr. 1 hit.
PROSITEPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBFR_SYNY3
AccessionPrimary (citable) accession number: P24602
Secondary accession number(s): P74531
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families