P22759 (BFR_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bacterioferritin
Short name=BFR
EC=1.16.3.1

Alternative name(s):
Cytochrome b-557.5

Gene names

Name:

bfr

Organism

Azotobacter vinelandii

Taxonomic identifier

354 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter group › Azotobacter

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Cofactor	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.
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

Keywords
Biological process	Iron storage
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW iron ion transport Inferred from electronic annotation. Source: InterPro
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

Bacterioferritin

PRO_0000192588

Regions

Domain

1 – 145

145

Ferritin-like diiron

Sites

Metal binding

18

1

Iron 1 By similarity

Metal binding

51

1

Iron 1 By similarity

Metal binding

51

1

Iron 2 By similarity

Metal binding

52

1

Iron (heme axial ligand); shared with dimeric partner By similarity

Metal binding

54

1

Iron 1 By similarity

Metal binding

94

1

Iron 2 By similarity

Metal binding

127

1

Iron 1 By similarity

Metal binding

127

1

Iron 2 By similarity

Metal binding

130

1

Iron 2 By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

156

Helix Strand Turn

Details...

Helix

5 – 34

30

Helix

38 – 64

27

Helix

83 – 110

28

Helix

114 – 144

31

Helix

146 – 151

6

Sequences

	Sequence		Length	Mass (Da)
	P22759 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: 468C2F059240A647	FASTA	156	18,105
	10 20 30 40 50 60 MKGDKIVIQH LNKILGNELI AINQYFLHAR MYEDWGLEKL GKHEYHESID EMKHADKLIK 70 80 90 100 110 120 RILFLEGLPN LQELGKLLIG EHTKEMLECD LKLEQAGLPD LKAAIAYCES VGDYASRELL 130 140 150 EDILESEEDH IDWLETQLDL IDKIGLENYL QSQMDE

References

[1]	"Unification of the ferritin family of proteins." Grossman M.J., Hinton S.M., Minak-Bernero V., Slaughter C., Stiefel E.I. Proc. Natl. Acad. Sci. U.S.A. 89:2419-2423(1992) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M83692 Genomic DNA. Translation: AAA22121.1.

PIR

A41983.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P22759.

SMR

P22759. Positions 1-155.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.20.1260.10. 1 hit.

InterPro

IPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]

Pfam

PF00210. Ferritin. 1 hit.
[Graphical view]

PIRSF

PIRSF002560. Bacterioferritin. 1 hit.

PRINTS

PR00601. BACFERRITIN.

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

TIGRFAMs

TIGR00754. bfr. 1 hit.

PROSITE

PS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22759.

Entry information

Entry name

BFR_AZOVI

Accession

Primary (citable) accession number: P22759

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program