UniProt functional annotation for P0ABD3



	UniProt functional annotation for P0ABD3

UniProt code: P0ABD3.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule. {ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073}.

Catalytic activity: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073, ECO:0000269|PubMed:19705876};

Cofactor: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:19391621}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. {ECO:0000269|PubMed:19391621};

Cofactor: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:19391621}; Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron- binding site within each subunit is known as the ferroxidase center. In BFR, the ferroxidase center appears to function as a true di-iron catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins. {ECO:0000269|PubMed:19391621};

Activity regulation: Iron oxidation is inhibited by Zn(2+), which binds at the ferroxidase center with a higher affinity that Fe(2+). The occupation of the ferroxidase center by Zn(2+) also severely restricts the ability of BFR to form an iron core. {ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073, ECO:0000269|PubMed:19705876}.

Subunit: Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited as a ferric-oxy-hydroxide mineral core. {ECO:0000269|PubMed:17077480, ECO:0000269|PubMed:18946693, ECO:0000269|PubMed:19439409, ECO:0000269|PubMed:19705876, ECO:0000269|PubMed:21215826, ECO:0000269|PubMed:7664064, ECO:0000269|PubMed:9867433}.

Mass spectrometry: Mass=18496; Mass_error=2; Method=Electrospray; Evidence={ECO:0000269|PubMed:7559480};

Miscellaneous: The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe(2+) binding and oxidation at the ferroxidase center.

Similarity: Belongs to the bacterioferritin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule. {ECO:0000269\|PubMed:10769150, ECO:0000269\|PubMed:14636073}.


Catalytic activity:		Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000269\|PubMed:10769150, ECO:0000269\|PubMed:14636073, ECO:0000269\|PubMed:19705876};
Cofactor:		Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269\|PubMed:19391621}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. {ECO:0000269\|PubMed:19391621};
Cofactor:		Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269\|PubMed:19391621}; Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron- binding site within each subunit is known as the ferroxidase center. In BFR, the ferroxidase center appears to function as a true di-iron catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins. {ECO:0000269\|PubMed:19391621};
Activity regulation:		Iron oxidation is inhibited by Zn(2+), which binds at the ferroxidase center with a higher affinity that Fe(2+). The occupation of the ferroxidase center by Zn(2+) also severely restricts the ability of BFR to form an iron core. {ECO:0000269\|PubMed:10769150, ECO:0000269\|PubMed:14636073, ECO:0000269\|PubMed:19705876}.
Subunit:		Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited as a ferric-oxy-hydroxide mineral core. {ECO:0000269\|PubMed:17077480, ECO:0000269\|PubMed:18946693, ECO:0000269\|PubMed:19439409, ECO:0000269\|PubMed:19705876, ECO:0000269\|PubMed:21215826, ECO:0000269\|PubMed:7664064, ECO:0000269\|PubMed:9867433}.
Mass spectrometry:		Mass=18496; Mass_error=2; Method=Electrospray; Evidence={ECO:0000269\|PubMed:7559480};
Miscellaneous:		The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe(2+) binding and oxidation at the ferroxidase center.
Similarity:		Belongs to the bacterioferritin family. {ECO:0000305}.