EC - Bacterial non-heme ferritin

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IntEnz Enzyme Nomenclature


Accepted name:
bacterial non-heme ferritin
Other names:
Systematic name:
Fe(II):oxygen oxidoreductase ([FeO(OH)]core-producing)



Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life. They are formed from two subunits that co-assemble in various ratios to form a spherical protein shell. Thousands of mineralized iron atoms are stored within the core of the structure. The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (23) [show] [UniProt]


  1. Hudson, A. J., Andrews, S. C., Hawkins, C., Williams, J. M., Izuhara, M., Meldrum, F. C., Mann, S., Harrison, P. M., Guest, J. R.
    Overproduction, purification and characterization of the Escherichia coli ferritin.
    Eur. J. Biochem. 218: 985-995 (1993). [PMID: 8281950]
  2. Stillman, T. J., Hempstead, P. D., Artymiuk, P. J., Andrews, S. C., Hudson, A. J., Treffry, A., Guest, J. R., Harrison, P. M.
    The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives.
    J. Mol. Biol. 307: 587-603 (2001). [PMID: 11254384]
  3. Bou-Abdallah, F., Yang, H., Awomolo, A., Cooper, B., Woodhall, M. R., Andrews, S. C., Chasteen, N. D.
    Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA).
    Biochemistry 53: 483-495 (2014). [PMID: 24380371]

[EC created 2014]