BFR_RHOCA
ID BFR_RHOCA Reviewed; 161 AA.
AC Q59738;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Bacterioferritin;
DE Short=BFR;
DE EC=1.16.3.1;
GN Name=bfr;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 938 / 37b4;
RX PubMed=8674981; DOI=10.1111/j.1574-6968.1996.tb08194.x;
RA Penfold C.N., Ringeling P.L., Davy S.L., Moore G.R., McEwan A.G., Spiro S.;
RT "Isolation, characterisation and expression of the bacterioferritin gene of
RT Rhodobacter capsulatus.";
RL FEMS Microbiol. Lett. 139:143-148(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=11752777; DOI=10.1107/s0907444901017267;
RA Cobessi D., Huang L.-S., Ban M., Pon N.G., Daldal F., Berry E.A.;
RT "The 2.6 A resolution structure of Rhodobacter capsulatus bacterioferritin
RT with metal-free dinuclear site and heme iron in a crystallographic 'special
RT position'.";
RL Acta Crystallogr. D 58:29-38(2002).
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;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
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 -!- 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 -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
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DR EMBL; Z54247; CAA91017.1; -; Genomic_DNA.
DR PIR; S48182; S48182.
DR RefSeq; WP_013066657.1; NZ_VIBE01000011.1.
DR PDB; 1JGC; X-ray; 2.60 A; A/B/C=1-161.
DR PDBsum; 1JGC; -.
DR AlphaFoldDB; Q59738; -.
DR SMR; Q59738; -.
DR GeneID; 31489850; -.
DR OMA; YQRLFHV; -.
DR EvolutionaryTrace; Q59738; -.
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; Heme; Iron; Iron storage; Metal-binding; Oxidoreductase.
FT CHAIN 1..161
FT /note="Bacterioferritin"
FT /id="PRO_0000192611"
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 BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
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 BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT HELIX 5..34
FT /evidence="ECO:0007829|PDB:1JGC"
FT HELIX 38..64
FT /evidence="ECO:0007829|PDB:1JGC"
FT HELIX 83..111
FT /evidence="ECO:0007829|PDB:1JGC"
FT HELIX 114..144
FT /evidence="ECO:0007829|PDB:1JGC"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:1JGC"
SQ SEQUENCE 161 AA; 18173 MW; 9E534CBC531EC709 CRC64;
MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE EMGHADKIIA
RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL YREARDYCAE VGDIVSKNIF
ESLITDEEGH VDFLETQISL YDRLGPQGFA LLNAAPMDAA E
