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7.3.2.5: ABC-type molybdate transporter

This is an abbreviated version!
For detailed information about ABC-type molybdate transporter, go to the full flat file.

Word Map on EC 7.3.2.5

Reaction

ATP
+
H2O
 +
molybdate-[molybdate-binding protein][side 1]
=
ADP
 +
phosphate
 +
molybdate[side 2]
 +
[molybdate-binding protein][side 1]

Synonyms

afModBCA, EC 3.6.3.29, HI1470/71, high-affinity molybdate transporter, hiMolBCA, low affinity molybdate transporter, mitochondrial molybdenum transporter, ModA, ModA/WtpA, ModABC, ModABC transporter, ModB, ModBC, ModBCA, ModC, MolA, MolB2C2, MolB2C2-A, MolBC-A, MolBCA, molybdate importer, molybdate transport system, molybdate transporter, molybdate transporter ATPase, molybdate- or tungstate-binding protein, molybdate-transporting ATPase, molybdate/tungstate ABC transporter, molybdenum tansporter 1, molybdenum transporter, MOP, More, MOT1, oxyanion permease, PerO, tungstate/molybdate-binding protein, type II molybdate importer, WtpABC

ECTree

     7 Translocases
         7.3 Catalysing the translocation of inorganic anions and their chelates
             7.3.2 Linked to the hydrolysis of a nucleoside triphosphate
                7.3.2.5 ABC-type molybdate transporter

Metals Ions

Metals Ions on EC 7.3.2.5 - ABC-type molybdate transporter

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdate
specific binding of tungstate or molybdate, involving residues Ser286, Thr320, Ser323, and Lys340, to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
Tungsten
specific binding of tungstate or molybdate, involving residues Ser286, Thr320, Ser323, and Lys340, to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview