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 27-MAR-2024, entry version 135. 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; Pseudomonadota; 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}. 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; 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; 511145-b3336; -. DR EnsemblBacteria; AAC76361; AAC76361; b3336. 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; YQRLFHV; -. DR OrthoDB; 9800505at2; -. DR PhylomeDB; P0ABD3; -. DR BioCyc; EcoCyc:EG10113-MONOMER; -. DR BioCyc; MetaCyc:EG10113-MONOMER; -. 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:CACAO. 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:0042803; F:protein homodimerization activity; IDA:EcoCyc. 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 NCBIfam; TIGR00754; bfr; 1. 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; 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 //