BFR_AZOVI
ID BFR_AZOVI Reviewed; 156 AA.
AC P22759;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Bacterioferritin;
DE Short=BFR;
DE EC=1.16.3.1;
DE AltName: Full=Cytochrome b-557.5;
GN Name=bfr;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1549605; DOI=10.1073/pnas.89.6.2419;
RA Grossman M.J., Hinton S.M., Minak-Bernero V., Slaughter C., Stiefel E.I.;
RT "Unification of the ferritin family of proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2419-2423(1992).
RN [2]
RP PROTEIN SEQUENCE OF 1-70.
RX PubMed=1904771; DOI=10.1016/0167-4838(91)90099-l;
RA Andrews S.C., Findlay J.B.C., Guest J.R., Harrison P.M., Keen J.N.,
RA Smith J.M.A.;
RT "Physical, chemical and immunological properties of the bacterioferritins
RT of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vinelandii.";
RL Biochim. Biophys. Acta 1078:111-116(1991).
CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+)
CC ions, oxidizes them by dioxygen to Fe(3+), and participates in the
CC subsequent Fe(3+) oxide mineral core formation within the central
CC cavity of the protein complex. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron-
CC binding site within each subunit is known as the ferroxidase center.
CC {ECO:0000250};
CC -!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers, that are
CC packed together to form an approximately spherical molecule with a
CC central cavity, in which large amounts of iron can be deposited.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
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DR EMBL; M83692; AAA22121.1; -; Genomic_DNA.
DR PIR; A41983; A41983.
DR RefSeq; WP_012700041.1; NZ_FPKM01000033.1.
DR PDB; 1SOF; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-156.
DR PDB; 2FKZ; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-155.
DR PDB; 2FL0; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-155.
DR PDBsum; 1SOF; -.
DR PDBsum; 2FKZ; -.
DR PDBsum; 2FL0; -.
DR AlphaFoldDB; P22759; -.
DR SMR; P22759; -.
DR PRIDE; P22759; -.
DR OMA; YQRLFHV; -.
DR EvolutionaryTrace; P22759; -.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR CDD; cd00907; Bacterioferritin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002024; Bacterioferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF002560; Bacterioferritin; 1.
DR PRINTS; PR00601; BACFERRITIN.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR00754; bfr; 1.
DR PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Iron storage;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..156
FT /note="Bacterioferritin"
FT /id="PRO_0000192588"
FT DOMAIN 1..145
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 18
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 52
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_note="ligand shared between dimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT HELIX 5..34
FT /evidence="ECO:0007829|PDB:2FKZ"
FT HELIX 38..64
FT /evidence="ECO:0007829|PDB:2FKZ"
FT HELIX 83..110
FT /evidence="ECO:0007829|PDB:2FKZ"
FT HELIX 114..144
FT /evidence="ECO:0007829|PDB:2FKZ"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:2FKZ"
SQ SEQUENCE 156 AA; 18105 MW; 468C2F059240A647 CRC64;
MKGDKIVIQH LNKILGNELI AINQYFLHAR MYEDWGLEKL GKHEYHESID EMKHADKLIK
RILFLEGLPN LQELGKLLIG EHTKEMLECD LKLEQAGLPD LKAAIAYCES VGDYASRELL
EDILESEEDH IDWLETQLDL IDKIGLENYL QSQMDE
