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 26-FEB-2020, entry version 97. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q59738; -. DR GeneID; 31489850; -. DR eggNOG; ENOG4108UQY; Bacteria. DR eggNOG; COG2193; LUCA. DR EvolutionaryTrace; Q59738; -. DR GO; GO:0005623; C:cell; IEA:GOC. 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 METAL 18 FT /note="Iron 1" FT METAL 51 FT /note="Iron 1" FT METAL 51 FT /note="Iron 2" FT METAL 52 FT /note="Iron (heme axial ligand); shared with dimeric FT partner" FT METAL 54 FT /note="Iron 1" FT METAL 94 FT /note="Iron 2" FT METAL 127 FT /note="Iron 1" FT METAL 127 FT /note="Iron 2" FT METAL 130 FT /note="Iron 2" FT HELIX 5..34 FT /evidence="ECO:0000244|PDB:1JGC" FT HELIX 38..64 FT /evidence="ECO:0000244|PDB:1JGC" FT HELIX 83..111 FT /evidence="ECO:0000244|PDB:1JGC" FT HELIX 114..144 FT /evidence="ECO:0000244|PDB:1JGC" FT HELIX 146..152 FT /evidence="ECO:0000244|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 //