ID BFR_RHOCA STANDARD; PRT; 161 AA. AC Q59738; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Bacterioferritin (BFR). GN Name=bfr; OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DSM 938 / 37b4; RX MEDLINE=96275893; PubMed=8674981; 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 MEDLINE=21620770; 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: May perform analogous functions in iron detoxification CC and storage to that of animal ferritins (By similarity). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer. CC -!- SUBUNIT: Oligomer of 24 identical subunits. CC -!- MISCELLANEOUS: The di-iron binding site functions as active site CC where iron ions are oxidized from iron(II) to iron(III) before CC they are stored. CC -!- SIMILARITY: Belongs to the bacterioferritin family. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. 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; -. DR PDB; 1JGC; 09-JAN-02. DR InterPro; IPR002024; Bacterioferritin. DR InterPro; IPR009078; Ferritin/RR_like. DR InterPro; IPR008331; Ferritin_Dps. DR InterPro; IPR009040; Ferritin_like. DR Pfam; PF00210; Ferritin; 1. DR PRINTS; PR00601; BACFERRITIN. DR ProDom; PD002269; Bacterioferritin; 1. DR TIGRFAMs; TIGR00754; bfr; 1. DR PROSITE; PS00549; BACTERIOFERRITIN; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. KW 3D-structure; Heme; Iron; Iron storage; Metal-binding. FT DOMAIN 1 145 Ferritin-like diiron. 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). 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. SQ SEQUENCE 161 AA; 18172 MW; 9E534CBC531EC709 CRC64; MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE EMGHADKIIA RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL YREARDYCAE VGDIVSKNIF ESLITDEEGH VDFLETQISL YDRLGPQGFA LLNAAPMDAA E //