ID   BFR_DESDA               Reviewed;         179 AA.
AC   Q93PP9; B8J0L2;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Bacterioferritin;
DE            Short=BFR;
DE            EC=1.16.3.1;
GN   Name=bfr; OrderedLocusNames=Ddes_1387;
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11454214; DOI=10.1046/j.1365-2958.2001.02509.x;
RA   da Costa P.N., Romao C.V., LeGall J., Xavier A.V., Melo E., Teixeira M.,
RA   Saraiva L.M.;
RT   "The genetic organization of Desulfovibrio desulphuricans ATCC 27774
RT   bacterioferritin and rubredoxin-2 genes: involvement of rubredoxin in iron
RT   metabolism.";
RL   Mol. Microbiol. 41:217-227(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 / DSM 6949 / MB;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   PARTIAL PROTEIN SEQUENCE, SUBUNIT, REDOX POTENTIOMETRY OF HEME, ABSORPTION
RP   SPECTROSCOPY, AND EPR SPECTROSCOPY.
RX   PubMed=10841764; DOI=10.1021/bi992525d;
RA   Romao C.V., Regalla M., Xavier A.V., Teixeira M., Liu M.-Y., Le Gall J.;
RT   "A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans
RT   ATCC 27774.";
RL   Biochemistry 39:6841-6849(2000).
RN   [4] {ECO:0000305}
RP   COFACTOR.
RX   PubMed=11034331; DOI=10.1016/s0014-5793(00)01939-6;
RA   Romao C.V., Louro R., Timkovich R., Lubben M., Liu M.Y., LeGall J.,
RA   Xavier A.V., Teixeira M.;
RT   "Iron-coproporphyrin III is a natural cofactor in bacterioferritin from the
RT   anaerobic bacterium Desulfovibrio desulfuricans.";
RL   FEBS Lett. 480:213-216(2000).
RN   [5] {ECO:0000305}
RP   CRYSTALLIZATION.
RX   PubMed=11173495; DOI=10.1107/s0907444900015286;
RA   Coelho A.V., Macedo S., Matias P.M., Thompson A.W., LeGall J.,
RA   Carrondo M.A.;
RT   "Structure determination of bacterioferritin from Desulfovibrio
RT   desulfuricans by the MAD method at the Fe K-edge.";
RL   Acta Crystallogr. D 57:326-329(2001).
RN   [6] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX   PubMed=12627224; DOI=10.1038/nsb909;
RA   Macedo S., Romao C.V., Mitchell E., Matias P.M., Liu M.Y., Xavier A.V.,
RA   LeGall J., Teixeira M., Lindley P., Carrondo M.A.;
RT   "The nature of the di-iron site in the bacterioferritin from Desulfovibrio
RT   desulfuricans.";
RL   Nat. Struct. Biol. 10:285-290(2003).
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.
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=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC         Evidence={ECO:0000269|PubMed:11034331};
CC       Note=Binds 1 Fe-coproporphyrin III group per dimer.
CC       {ECO:0000269|PubMed:11034331};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:11034331};
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:0000269|PubMed:11034331};
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:0000269|PubMed:10841764}.
CC   -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
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DR   EMBL; AF321851; AAK60120.1; -; Genomic_DNA.
DR   EMBL; CP001358; ACL49289.1; -; Genomic_DNA.
DR   PDB; 1NF4; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-179.
DR   PDB; 1NF6; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-179.
DR   PDB; 1NFV; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-179.
DR   PDBsum; 1NF4; -.
DR   PDBsum; 1NF6; -.
DR   PDBsum; 1NFV; -.
DR   AlphaFoldDB; Q93PP9; -.
DR   SMR; Q93PP9; -.
DR   STRING; 525146.Ddes_1387; -.
DR   KEGG; dds:Ddes_1387; -.
DR   eggNOG; COG2193; Bacteria.
DR   HOGENOM; CLU_104506_1_0_7; -.
DR   BRENDA; 1.16.3.1; 1905.
DR   EvolutionaryTrace; Q93PP9; -.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006880; P:intracellular sequestering of iron ion; NAS:UniProtKB.
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   PANTHER; PTHR30295; BACTERIOFERRITIN; 1.
DR   PANTHER; PTHR30295:SF0; BACTERIOFERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF002560; Bacterioferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   SUPFAM; SSF47240; Ferritin-like; 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..179
FT                   /note="Bacterioferritin"
FT                   /id="PRO_0000192591"
FT   DOMAIN          1..150
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         23
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         57
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
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         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         99
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         132
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         132
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   HELIX           5..39
FT                   /evidence="ECO:0007829|PDB:1NFV"
FT   HELIX           43..69
FT                   /evidence="ECO:0007829|PDB:1NFV"
FT   HELIX           88..115
FT                   /evidence="ECO:0007829|PDB:1NFV"
FT   HELIX           119..149
FT                   /evidence="ECO:0007829|PDB:1NFV"
FT   HELIX           151..157
FT                   /evidence="ECO:0007829|PDB:1NFV"
SQ   SEQUENCE   179 AA;  19881 MW;  09E3387462FED3A3 CRC64;
     MAGNREDRKA KVIEVLNKAR AMELHAIHQY MNQHYSLDDM DYGELAANMK LIAIDEMRHA
     ENFAERIKEL GGEPTTQKEG KVVTGQAVPV IYESDADQED ATIEAYSQFL KVCKEQGDIV
     TARLFERIIE EEQAHLTYYE NIGSHIKNLG DTYLAKIAGT PSSTGTASKG FVTATPAAE
//