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{{enzyme
| Name = iron-chelate-transporting ATPase
| EC_number = 3.6.3.34
| CAS_number =
| IUBMB_EC_number = 3/6/3/34
| GO_code = 0015623
| image =
| width =
| caption =
}}
In [[enzymology]], an '''iron-chelate-transporting ATPase''' ({{EC number|3.6.3.34}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:ATP + H<sub>2</sub>O + iron chelateout <math>\rightleftharpoons</math> ADP + phosphate + iron chelatein

The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[water|H<sub>2</sub>O]], and [[iron chelate]], whereas its 3 [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]], [[phosphate]], and [[iron chelate]].

This enzyme belongs to the family of [[hydrolase]]s, 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==

As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1L2P}}, {{PDB link|1L6T}}, and {{PDB link|2IHY}}.

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

[[Category:EC 3.6.3]]
[[Category:Enzymes of known structure]]

{{hydrolase-stub}}

FAD diphosphatase - Revision history

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