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 02-NOV-2016, entry version 86. 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., RA Spiro S.; RT "Isolation, characterisation and expression of the bacterioferritin RT gene of Rhodobacter capsulatus."; RL FEMS Microbiol. Lett. 139:143-148(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=11752777; 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 RT bacterioferritin with metal-free dinuclear site and heme iron in a RT crystallographic 'special position'."; RL Acta Crystallogr. D 58:29-38(2002). CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds CC Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates CC in the subsequent Fe(3+) oxide mineral core formation within the CC central cavity of the protein complex. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. 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 CC center.; CC -!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers, that CC are packed together to form an approximately spherical molecule CC with a central cavity, in which large amounts of iron can be CC deposited. CC -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000255|PROSITE-ProRule:PRU00085}. 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 PDB; 1JGC; X-ray; 2.60 A; A/B/C=1-161. DR PDBsum; 1JGC; -. DR ProteinModelPortal; Q59738; -. DR SMR; Q59738; -. DR STRING; 272942.RCAP_rcc00913; -. DR eggNOG; ENOG4108UQY; Bacteria. DR eggNOG; COG2193; LUCA. DR HOGENOM; HOG000262383; -. 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; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. 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 Bacterioferritin. FT /FTId=PRO_0000192611. FT DOMAIN 1 145 Ferritin-like diiron. FT {ECO:0000255|PROSITE-ProRule:PRU00085}. FT METAL 18 18 Iron 1. FT METAL 51 51 Iron 1. FT METAL 51 51 Iron 2. FT METAL 52 52 Iron (heme axial ligand); shared with FT dimeric partner. FT METAL 54 54 Iron 1. FT METAL 94 94 Iron 2. FT METAL 127 127 Iron 1. FT METAL 127 127 Iron 2. FT METAL 130 130 Iron 2. FT HELIX 5 34 {ECO:0000244|PDB:1JGC}. FT HELIX 38 64 {ECO:0000244|PDB:1JGC}. FT HELIX 83 111 {ECO:0000244|PDB:1JGC}. FT HELIX 114 144 {ECO:0000244|PDB:1JGC}. FT HELIX 146 152 {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 //