BFR_DESDA
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 03-AUG-2022, entry version 112.
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; Proteobacteria; Deltaproteobacteria; 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 RefSeq; WP_012625013.1; NC_011883.1.
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 EnsemblBacteria; ACL49289; ACL49289; Ddes_1387.
DR KEGG; dds:Ddes_1387; -.
DR eggNOG; COG2193; Bacteria.
DR HOGENOM; CLU_104506_1_0_7; -.
DR OMA; NEEEHFH; -.
DR OrthoDB; 1890523at2; -.
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 Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF002560; Bacterioferritin; 1.
DR PRINTS; PR00601; BACFERRITIN.
DR SUPFAM; SSF47240; SSF47240; 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
