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Literature summary extracted from

  • Vigonsky, E.; Ovcharenko, E.; Lewinson, O.
    Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins (2013), Proc. Natl. Acad. Sci. USA, 110, 5440-5445.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.3.2.5
-
Haemophilus influenzae
7.3.2.5
-
Archaeoglobus fulgidus

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.3.2.5 vanadate
-
Archaeoglobus fulgidus
7.3.2.5 vanadate
-
Haemophilus influenzae
7.3.2.6 vanadate
-
Archaeoglobus fulgidus
7.3.2.6 vanadate
-
Haemophilus influenzae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.3.2.5 additional information
-
additional information transporter component interaction kinetics and affinities, overview Haemophilus influenzae
7.3.2.5 additional information
-
additional information transporter component interaction kinetics and affinities, overview Archaeoglobus fulgidus
7.3.2.6 additional information
-
additional information transporter component interaction kinetics and affinities, overview Haemophilus influenzae
7.3.2.6 additional information
-
additional information transporter component interaction kinetics and affinities, overview Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.3.2.5 Mg2+ required Haemophilus influenzae
7.3.2.5 Mg2+ required Archaeoglobus fulgidus
7.3.2.6 Mg2+ required Haemophilus influenzae
7.3.2.6 Mg2+ required Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.3.2.5 ATP + H2O + molybdate/out Haemophilus influenzae
-
ADP + phosphate + molybdate/in
-
?
7.3.2.5 ATP + H2O + molybdate/out Archaeoglobus fulgidus
-
ADP + phosphate + molybdate/in
-
?
7.3.2.5 additional information Haemophilus influenzae the enzyme is an ABC importer with substrate specificity for molybdate and tungstate ?
-
?
7.3.2.5 additional information Archaeoglobus fulgidus the enzyme is an ABC importer with substrate specificity for molybdate and tungstate ?
-
?
7.3.2.6 ATP + H2O + tungstate[side 1] Haemophilus influenzae
-
ADP + phosphate + tungstate[side 2]
-
?
7.3.2.6 ATP + H2O + tungstate[side 1] Archaeoglobus fulgidus
-
ADP + phosphate + tungstate[side 2]
-
?
7.3.2.6 additional information Haemophilus influenzae the enzyme is an ABC importer with substrate specificity for molybdate and tungstate ?
-
?
7.3.2.6 additional information Archaeoglobus fulgidus the enzyme is an ABC importer with substrate specificity for molybdate and tungstate ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
7.3.2.5 Archaeoglobus fulgidus
-
-
-
7.3.2.5 Archaeoglobus fulgidus O30144 ModC
-
7.3.2.5 Haemophilus influenzae
-
-
-
7.3.2.5 Haemophilus influenzae Q4QJQ0 ATPase ModC
-
7.3.2.6 Archaeoglobus fulgidus
-
-
-
7.3.2.6 Haemophilus influenzae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.3.2.5
-
Haemophilus influenzae
7.3.2.5
-
Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.3.2.5 ATP + H2O + molybdate/out
-
Haemophilus influenzae ADP + phosphate + molybdate/in
-
?
7.3.2.5 ATP + H2O + molybdate/out
-
Archaeoglobus fulgidus ADP + phosphate + molybdate/in
-
?
7.3.2.5 additional information the enzyme is an ABC importer with substrate specificity for molybdate and tungstate Haemophilus influenzae ?
-
?
7.3.2.5 additional information the enzyme is an ABC importer with substrate specificity for molybdate and tungstate Archaeoglobus fulgidus ?
-
?
7.3.2.5 additional information component afMolA binds its substrates with high affinity, the affinity toward tungstate is higher. Binding of molybdate by afModA is endothermic, while that of tungstate is exothermic. Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, modeling of the mechanism, overview Archaeoglobus fulgidus ?
-
?
7.3.2.5 additional information component hiMolA binds its substrates with low affinity.Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, overview Haemophilus influenzae ?
-
?
7.3.2.6 ATP + H2O + tungstate[side 1]
-
Haemophilus influenzae ADP + phosphate + tungstate[side 2]
-
?
7.3.2.6 ATP + H2O + tungstate[side 1]
-
Archaeoglobus fulgidus ADP + phosphate + tungstate[side 2]
-
?
7.3.2.6 additional information the enzyme is an ABC importer with substrate specificity for molybdate and tungstate Haemophilus influenzae ?
-
?
7.3.2.6 additional information the enzyme is an ABC importer with substrate specificity for molybdate and tungstate Archaeoglobus fulgidus ?
-
?
7.3.2.6 additional information component afMolA binds its substrates with high affinity, the affinity toward tungstate is higher. Binding of molybdate by afModA is endothermic, while that of tungstate is exothermic. Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, modeling of the mechanism, overview Archaeoglobus fulgidus ?
-
?
7.3.2.6 additional information component hiMolA binds its substrates with low affinity. Reconstitution of the detergent-free enzyme components BCA into liposomes and analysis of interaction between proteins BC and protein A, effects of nucleotides and substrates on the interaction, overview Haemophilus influenzae ?
-
?

Subunits

EC Number Subunits Comment Organism
7.3.2.5 More the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold Haemophilus influenzae
7.3.2.5 More the enzyme components afModBC have 12 transmembrane alpha-helices that adopt the characteristic fold of type I ABC importers Archaeoglobus fulgidus
7.3.2.6 More the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold Haemophilus influenzae
7.3.2.6 More the enzyme components afModBC have 12 transmembrane alpha-helices that adopt the characteristic fold of type I ABC importers Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
7.3.2.5 afModBCA
-
Archaeoglobus fulgidus
7.3.2.5 hiMolBCA
-
Haemophilus influenzae
7.3.2.5 ModBCA
-
Archaeoglobus fulgidus
7.3.2.5 MolBCA
-
Haemophilus influenzae
7.3.2.5 molybdate/tungstate ABC transporter
-
Haemophilus influenzae
7.3.2.5 molybdate/tungstate ABC transporter
-
Archaeoglobus fulgidus
7.3.2.6 afModBCA
-
Archaeoglobus fulgidus
7.3.2.6 hiMolBCA
-
Haemophilus influenzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3.2.5 7.5
-
assay at Haemophilus influenzae
7.3.2.5 7.5
-
assay at Archaeoglobus fulgidus
7.3.2.6 7.5
-
assay at Haemophilus influenzae
7.3.2.6 7.5
-
assay at Archaeoglobus fulgidus

General Information

EC Number General Information Comment Organism
7.3.2.5 additional information three-dimensional structure modeling Haemophilus influenzae
7.3.2.5 additional information three-dimensional structure modeling Archaeoglobus fulgidus
7.3.2.5 physiological function afModBCA is a high-affinity transport system for molybdate and tungstate anions Archaeoglobus fulgidus
7.3.2.6 additional information three-dimensional structure modeling Haemophilus influenzae
7.3.2.6 additional information three-dimensional structure modeling Archaeoglobus fulgidus
7.3.2.6 physiological function afModBCA is a high-affinity transport system for molybdate and tungstate anions Archaeoglobus fulgidus