BFR_ECOLI
ID BFR_ECOLI Reviewed; 158 AA.
AC P0ABD3; O68931; P11056; Q2M701;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Bacterioferritin;
DE Short=BFR;
DE EC=1.16.3.1;
DE AltName: Full=Cytochrome b-1;
DE AltName: Full=Cytochrome b-557;
GN Name=bfr; OrderedLocusNames=b3336, JW3298;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2661540; DOI=10.1128/jb.171.7.3940-3947.1989;
RA Andrews S.C., Harrison P.M., Guest J.R.;
RT "Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of
RT Escherichia coli K-12.";
RL J. Bacteriol. 171:3940-3947(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ECOR 30;
RA Noorani S.M., Lindahl L., Zengel J.M.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-87.
RC STRAIN=K12;
RX PubMed=2644932; DOI=10.1016/s0006-291x(89)80075-0;
RA Andrews S.C., Smith J.M.A., Guest J.R., Harrison P.M.;
RT "Amino acid sequence of the bacterioferritin (cytochrome b1) of Escherichia
RT coli-K12.";
RL Biochem. Biophys. Res. Commun. 158:489-496(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-158.
RC STRAIN=K12;
RX PubMed=7959070; DOI=10.1016/0378-1119(94)90851-6;
RA Whitchurch C.B., Mattick J.S.;
RT "Escherichia coli contains a set of genes homologous to those involved in
RT protein secretion, DNA uptake and the assembly of type-4 fimbriae in other
RT bacteria.";
RL Gene 150:9-15(1994).
RN [7]
RP HEME-BINDING, MASS SPECTROMETRY, AND MUTAGENESIS OF MET-31; MET-52 AND
RP MET-86.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=7559480; DOI=10.1074/jbc.270.40.23268;
RA Andrews S.C., Le Brun N.E., Barynin V., Thomson A.J., Moore G.R.,
RA Guest J.R., Harrison P.M.;
RT "Site-directed replacement of the coaxial heme ligands of bacterioferritin
RT generates heme-free variants.";
RL J. Biol. Chem. 270:23268-23274(1995).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=10769150; DOI=10.1021/bi992631f;
RA Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.;
RT "The iron oxidation and hydrolysis chemistry of Escherichia coli
RT bacterioferritin.";
RL Biochemistry 39:4915-4923(2000).
RN [10]
RP FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-18; GLU-127 AND
RP HIS-130.
RX PubMed=14636073; DOI=10.1021/bi035253u;
RA Baaghil S., Lewin A., Moore G.R., Le Brun N.E.;
RT "Core formation in Escherichia coli bacterioferritin requires a functional
RT ferroxidase center.";
RL Biochemistry 42:14047-14056(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE
RP IONS.
RX PubMed=7664064; DOI=10.1038/nsb0794-453;
RA Frolow F., Kalb A.J., Yariv J.;
RT "Structure of a unique twofold symmetric haem-binding site.";
RL Nat. Struct. Biol. 1:453-460(1994).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE
RP IONS, AND SUBUNIT.
RX PubMed=9867433; DOI=10.1107/s0907444997006811;
RA Dautant A., Meyer J.-B., Yariv J., Precigoux G., Sweet R.M., Kalb A.J.,
RA Frolow F.;
RT "Structure of a monoclinic crystal form of cytochrome b1 (bacterioferritin)
RT from E. coli.";
RL Acta Crystallogr. D 54:16-24(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH HEME; IRON AND ZINC
RP IONS.
RC STRAIN=B / BL21;
RX PubMed=17077480; DOI=10.1107/s1744309106039583;
RA van Eerde A., Wolterink-van Loo S., van der Oost J., Dijkstra B.W.;
RT "Fortuitous structure determination of 'as-isolated' Escherichia coli
RT bacterioferritin in a novel crystal form.";
RL Acta Crystallogr. F 62:1061-1066(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN
RP COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=19705876; DOI=10.1021/bi900869x;
RA Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.;
RT "Monitoring the iron status of the ferroxidase center of Escherichia coli
RT bacterioferritin using fluorescence spectroscopy.";
RL Biochemistry 48:9031-9039(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF METAL-FREE APOPROTEIN AND IN
RP COMPLEXES WITH ZN(2+); FE(2+); FE(3+) AND HEME, COFACTOR, INTERNAL SURFACE
RP IRON-BINDING SITE, MUTAGENESIS OF HIS-46 AND ASP-50, AND MECHANISM OF IRON
RP MINERALIZATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=19391621; DOI=10.1021/ja8093444;
RA Crow A., Lawson T.L., Lewin A., Moore G.R., Le Brun N.E.;
RT "Structural basis for iron mineralization by bacterioferritin.";
RL J. Am. Chem. Soc. 131:6808-6813(2009).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ARG-128/ARG-135 DIMER IN
RP COMPLEX WITH HEME AND ZINC IONS.
RX PubMed=19439409; DOI=10.1074/jbc.m901747200;
RA Wong S.G., Tom-Yew S.A., Lewin A., Le Brun N.E., Moore G.R., Murphy M.E.,
RA Mauk A.G.;
RT "Structural and mechanistic studies of a stabilized subunit dimer variant
RT of Escherichia coli bacterioferritin identify residues required for core
RT formation.";
RL J. Biol. Chem. 284:18873-18881(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH HEME AND ZINC IONS.
RC STRAIN=B / BL21;
RX PubMed=18946693; DOI=10.1007/s00775-008-0438-8;
RA Willies S.C., Isupov M.N., Garman E.F., Littlechild J.A.;
RT "The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia
RT coli bacterioferritin.";
RL J. Biol. Inorg. Chem. 14:201-207(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=21215826; DOI=10.1016/j.bbapap.2010.12.017;
RA Antonyuk S.V., Hough M.A.;
RT "Monitoring and validating active site redox states in protein crystals.";
RL Biochim. Biophys. Acta 1814:778-784(2011).
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. The mineralized iron core can contain as
CC many as 2700 iron atoms/24-meric molecule.
CC {ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073}.
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 Evidence={ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073,
CC ECO:0000269|PubMed:19705876};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:19391621};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000269|PubMed:19391621};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:19391621};
CC Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron-
CC binding site within each subunit is known as the ferroxidase center. In
CC BFR, the ferroxidase center appears to function as a true di-iron
CC catalytic cofactor, rather than as a pore for the transfer of iron into
CC the central cavity, as found for eukaryotic ferritins.
CC {ECO:0000269|PubMed:19391621};
CC -!- ACTIVITY REGULATION: Iron oxidation is inhibited by Zn(2+), which binds
CC at the ferroxidase center with a higher affinity that Fe(2+). The
CC occupation of the ferroxidase center by Zn(2+) also severely restricts
CC the ability of BFR to form an iron core. {ECO:0000269|PubMed:10769150,
CC ECO:0000269|PubMed:14636073, ECO:0000269|PubMed:19705876}.
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 as a
CC ferric-oxy-hydroxide mineral core. {ECO:0000269|PubMed:17077480,
CC ECO:0000269|PubMed:18946693, ECO:0000269|PubMed:19439409,
CC ECO:0000269|PubMed:19705876, ECO:0000269|PubMed:21215826,
CC ECO:0000269|PubMed:7664064, ECO:0000269|PubMed:9867433}.
CC -!- INTERACTION:
CC P0ABD3; P0ABD3: bfr; NbExp=2; IntAct=EBI-907496, EBI-907496;
CC -!- MASS SPECTROMETRY: Mass=18496; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7559480};
CC -!- MISCELLANEOUS: The internal surface iron site that binds iron 3 is
CC important for the mineralization phase but not for Fe(2+) binding and
CC oxidation at the ferroxidase center.
CC -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
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DR EMBL; M27176; AAC13987.1; -; mRNA.
DR EMBL; AF058450; AAC14288.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58133.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76361.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77955.1; -; Genomic_DNA.
DR EMBL; L28106; AAC36929.1; -; Genomic_DNA.
DR PIR; JV0032; FREC.
DR RefSeq; NP_417795.1; NC_000913.3.
DR RefSeq; WP_000675504.1; NZ_STEB01000038.1.
DR PDB; 1BCF; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 1BFR; X-ray; 2.94 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-158.
DR PDB; 2HTN; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-158.
DR PDB; 2VXI; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 2Y3Q; X-ray; 1.55 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E1J; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E1L; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E1M; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E1N; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E1O; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E1P; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E1Q; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 3E2C; X-ray; 1.80 A; A/B=1-158.
DR PDB; 3GHQ; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 4CVP; X-ray; 2.11 A; A=1-158.
DR PDB; 4CVR; X-ray; 1.10 A; A=1-158.
DR PDB; 4CVS; X-ray; 1.39 A; A=1-158.
DR PDB; 4CVT; X-ray; 1.79 A; A=1-158.
DR PDB; 4U3G; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 4XKS; X-ray; 1.57 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 4XKT; X-ray; 1.82 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 4XKU; X-ray; 1.78 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 5XGO; X-ray; 1.99 A; A/B/C/D/E/F/G/H/I/J/K/L=138-158.
DR PDB; 6P8K; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDB; 6P8L; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDBsum; 1BCF; -.
DR PDBsum; 1BFR; -.
DR PDBsum; 2HTN; -.
DR PDBsum; 2VXI; -.
DR PDBsum; 2Y3Q; -.
DR PDBsum; 3E1J; -.
DR PDBsum; 3E1L; -.
DR PDBsum; 3E1M; -.
DR PDBsum; 3E1N; -.
DR PDBsum; 3E1O; -.
DR PDBsum; 3E1P; -.
DR PDBsum; 3E1Q; -.
DR PDBsum; 3E2C; -.
DR PDBsum; 3GHQ; -.
DR PDBsum; 4CVP; -.
DR PDBsum; 4CVR; -.
DR PDBsum; 4CVS; -.
DR PDBsum; 4CVT; -.
DR PDBsum; 4U3G; -.
DR PDBsum; 4XKS; -.
DR PDBsum; 4XKT; -.
DR PDBsum; 4XKU; -.
DR PDBsum; 5XGO; -.
DR PDBsum; 6P8K; -.
DR PDBsum; 6P8L; -.
DR AlphaFoldDB; P0ABD3; -.
DR SMR; P0ABD3; -.
DR BioGRID; 4262466; 23.
DR DIP; DIP-36167N; -.
DR IntAct; P0ABD3; 3.
DR STRING; 511145.b3336; -.
DR jPOST; P0ABD3; -.
DR PaxDb; P0ABD3; -.
DR PRIDE; P0ABD3; -.
DR EnsemblBacteria; AAC76361; AAC76361; b3336.
DR EnsemblBacteria; BAE77955; BAE77955; BAE77955.
DR GeneID; 58459569; -.
DR GeneID; 947839; -.
DR KEGG; ecj:JW3298; -.
DR KEGG; eco:b3336; -.
DR PATRIC; fig|1411691.4.peg.3395; -.
DR EchoBASE; EB0111; -.
DR eggNOG; COG2193; Bacteria.
DR HOGENOM; CLU_104506_2_0_6; -.
DR InParanoid; P0ABD3; -.
DR OMA; TPEMLKC; -.
DR PhylomeDB; P0ABD3; -.
DR BioCyc; EcoCyc:EG10113-MON; -.
DR BioCyc; MetaCyc:EG10113-MON; -.
DR BRENDA; 1.16.3.1; 2026.
DR EvolutionaryTrace; P0ABD3; -.
DR PRO; PR:P0ABD3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; NAS:EcoliWiki.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:EcoCyc.
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; Direct protein sequencing; Heme; Iron; Iron storage;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..158
FT /note="Bacterioferritin"
FT /id="PRO_0000192592"
FT DOMAIN 1..145
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 18
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 46
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 52
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085,
FT ECO:0000269|PubMed:17077480"
FT VARIANT 5..7
FT /note="TKV -> VKI (in strain: ECOR 30)"
FT VARIANT 38
FT /note="K -> M (in strain: ECOR 30)"
FT VARIANT 57
FT /note="R -> K (in strain: ECOR 30)"
FT VARIANT 68
FT /note="L -> I (in strain: ECOR 30)"
FT VARIANT 78
FT /note="N -> G (in strain: ECOR 30)"
FT VARIANT 88
FT /note="R -> Q (in strain: ECOR 30)"
FT VARIANT 92
FT /note="A -> R (in strain: ECOR 30)"
FT VARIANT 96
FT /note="D -> E (in strain: ECOR 30)"
FT VARIANT 100
FT /note="N -> D (in strain: ECOR 30)"
FT VARIANT 106
FT /note="G -> A (in strain: ECOR 30)"
FT VARIANT 125
FT /note="R -> A (in strain: ECOR 30)"
FT VARIANT 142..144
FT /note="QKM -> GKI (in strain: ECOR 30)"
FT VARIANT 152..158
FT /note="AQIREEG -> SQIKVKD (in strain: ECOR 30)"
FT MUTAGEN 18
FT /note="E->A: Highly decreased Fe(2+) oxidation activity. Is
FT also severely restricted in its ability to lay down an iron
FT core."
FT /evidence="ECO:0000269|PubMed:14636073"
FT MUTAGEN 31
FT /note="M->H,L: No loss of heme binding."
FT /evidence="ECO:0000269|PubMed:7559480"
FT MUTAGEN 46
FT /note="H->A: Fe(2+)-binding and single turnover oxidation
FT at the ferroxidase center occur normally but iron
FT mineralization within the cavity is significantly
FT impaired."
FT /evidence="ECO:0000269|PubMed:19391621"
FT MUTAGEN 50
FT /note="D->A: Fe(2+)-binding and single turnover oxidation
FT at the ferroxidase center occur normally but iron
FT mineralization within the cavity is significantly
FT impaired."
FT /evidence="ECO:0000269|PubMed:19391621"
FT MUTAGEN 52
FT /note="M->H,L: Loss of heme binding. Is still capable of
FT accumulating iron."
FT /evidence="ECO:0000269|PubMed:7559480"
FT MUTAGEN 86
FT /note="M->L: No loss of heme binding."
FT /evidence="ECO:0000269|PubMed:7559480"
FT MUTAGEN 127
FT /note="E->Q: Decreased Fe(2+) oxidation activity. Is also
FT affected in its ability to lay down an iron core."
FT /evidence="ECO:0000269|PubMed:14636073"
FT MUTAGEN 130
FT /note="H->E: Decreased Fe(2+) oxidation activity. Is also
FT severely restricted in its ability to lay down an iron
FT core."
FT /evidence="ECO:0000269|PubMed:14636073"
FT CONFLICT 53
FT /note="K -> M (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..34
FT /evidence="ECO:0007829|PDB:4CVR"
FT HELIX 38..64
FT /evidence="ECO:0007829|PDB:4CVR"
FT HELIX 83..110
FT /evidence="ECO:0007829|PDB:4CVR"
FT HELIX 114..144
FT /evidence="ECO:0007829|PDB:4CVR"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:4CVR"
SQ SEQUENCE 158 AA; 18495 MW; A6C86CE1CD8F865A CRC64;
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID EMKHADRYIE
RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN LREAIGYADS VHDYVSRDMM
IEILRDEEGH IDWLETELDL IQKMGLQNYL QAQIREEG
