Iron-chelate-transporting ATPase

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iron-chelate-transporting ATPase
Identifiers
EC no.3.6.3.34
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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In enzymology, an iron-chelate-transporting ATPase (EC 3.6.3.34) is an enzyme that catalyzes the chemical reaction

ATP + H2O + iron chelateout ADP + phosphate + iron chelatein

The 3 substrates of this enzyme are ATP, H2O, and iron chelate, whereas its 3 products are ADP, phosphate, and iron chelate.

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (iron-chelate-importing). This enzyme participates in abc transporters - general.

Structural studies[edit]

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1L2P, 1L6T, and 2IHY.

References[edit]

  • Shea CM, McIntosh MA (1991). "Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli". Mol. Microbiol. 5 (6): 1415–28. doi:10.1111/j.1365-2958.1991.tb00788.x. PMID 1838574. S2CID 25193069.
  • Koster W, Bohm B (1992). "Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport". Mol. Gen. Genet. 232 (3): 399–407. doi:10.1007/bf00266243. PMID 1588908. S2CID 28286920.
  • Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr (1995). "Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases". Res. Microbiol. 146 (4): 271–8. doi:10.1016/0923-2508(96)81050-3. PMID 7569321.
  • Saier MH Jr (1998). "Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya". Adv. Microb. Physiol. Advances in Microbial Physiology. 40: 81–136. doi:10.1016/S0065-2911(08)60130-7. ISBN 9780120277407. PMID 9889977.
  • Mademidis A, Koster W (1998). "Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake". Mol. Gen. Genet. 258 (1–2): 156–65. doi:10.1007/s004380050718. PMID 9613584. S2CID 25378659.