| EC |
7.2.2.18 |
| Accepted name: |
ABC-type ferric citrate transporter |
| Reaction: |
ATP + H2O + Fe3+-dicitrate-[dicitrate-binding protein][side 1] = ADP + phosphate + Fe3+-dicitrate[side 2] + [dicitrate-binding protein][side 1] |
| Other name(s): |
ferric citrate transporting ATPase; ferric citrate ABC transporter; fecBCDE (gene names) |
| Systematic name: |
ATP phosphohydrolase (ABC-type, iron(III) dicitrate-importing) |
| Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichia coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of Fe3+-citrate in the form of a mononuclear (containing one iron(III) ion and two citrate molecules) or dinuclear (containing 2 iron(III) ions) complexes. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Staudenmaier, H., Van Hove, B., Yaraghi, Z. and Braun, V. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. J. Bacteriol. 171 (1989) 2626–2633. [PMID: 2651410] |
| 2. |
Banerjee, S., Paul, S., Nguyen, L.T., Chu, B.C. and Vogel, H.J. FecB, a periplasmic ferric-citrate transporter from E. coli, can bind different forms of ferric-citrate as well as a wide variety of metal-free and metal-loaded tricarboxylic acids. Metallomics 8 (2016) 125–133. [PMID: 26600288] |
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| [EC 7.2.2.18 created 2000 as EC 3.6.3.34, part transferred 2018 to EC 7.2.2.18] |
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