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Information on EC 7.3.2.5 - ABC-type molybdate transporter and Organism(s) Haemophilus influenzae and UniProt Accession Q57399
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7.3.2.5 ABC-type molybdate transporterIUBMB 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, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of molybdate and tungstate. Does not undergo phosphorylation during the transport process.
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The taxonomic range for the selected organisms is: Haemophilus influenzae
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
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molybdate-[molybdate-binding protein][side 1]
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[molybdate-binding protein][side 1]
Synonyms
modabc, molybdate transporter, high-affinity molybdate transporter, modbc, molybdate transport system, molbc-a, molybdenum transporter, molybdate importer, moda/wtpa, wtpabc, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ModABC
molybdate transport system
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molybdate-transporting ATPase
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ModABC
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, molybdate-importing)
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, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of molybdate and tungstate. Does not undergo phosphorylation during the transport process.
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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additional information
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the MolA binding protein binds molybdate and tungstate but not other oxyanions such as sulfate and phosphate, it is thus a class III molybdate binding protein
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additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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additional information
?
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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
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additional information
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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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
additional information
?
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the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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transporter component interaction kinetics and affinities, overview
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additional information
additional information
transporter component interaction kinetics and affinities, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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periplasmic binding protein MolA delivers substrate to the ABC transporter MolB2C2
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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structure of MolA falls into the cluster A of a class III periplasmic binding protein with two topologically similar globular domains, domain I and II correspond to residues 1-175 and 197-322, respectively, MolA topology and binding coordination, overview
additional information
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the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold
additional information
the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MolA bound to tungstate and molybdate, X-ray diffraction structure determination and analysis at 1.6 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grunden, A.M.; Shanmugam, K.T.
Molybdate transport and regulation in bacteria
Arch. Microbiol.
168
345-354
1997
Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Escherichia coli, Haemophilus influenzae, Rhodobacter capsulatus
Self, W.T.; Grunden, A.M.; Hasona, A.; Shanmugam, K.T.
Molybdate transport
Res. Microbiol.
152
311-321
2001
Azotobacter vinelandii, Aeropyrum pernix, Synechocystis sp., Aquifex aeolicus, Paenarthrobacter nicotinovorans, Bacillus subtilis, Campylobacter jejuni, Deinococcus radiodurans, Escherichia coli, Haemophilus influenzae, Haloferax volcanii, Helicobacter pylori, Methanothermobacter thermautotrophicus, Methanopyrus kandleri, Mycobacterium tuberculosis, Pseudomonas aeruginosa, Pyrococcus abyssi, Pyrococcus furiosus, Pyrococcus horikoshii, Rhodobacter capsulatus, Staphylococcus carnosus, Streptomyces coelicolor, Vibrio cholerae serotype O1
Tirado-Lee, L.; Lee, A.; Rees, D.C.; Pinkett, H.W.
Classification of a Haemophilus influenzae ABC transporter HI1470/71 through its cognate molybdate periplasmic binding protein, MolA
Structure
19
1701-1710
2011
Haemophilus influenzae
Rice, A.J.; Alvarez, F.J.; Schultz, K.M.; Klug, C.S.; Davidson, A.L.; Pinkett, H.W.
EPR spectroscopy of MolB2C2-a reveals mechanism of transport for a bacterial type II molybdate importer
J. Biol. Chem.
288
21228-21235
2013
Haemophilus influenzae
Rice, A.J.; Harrison, A.; Alvarez, F.J.; Davidson, A.L.; Pinkett, H.W.
Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment
J. Biol. Chem.
289
15005-15013
2014
Haemophilus influenzae (Q57399), Haemophilus influenzae, Haemophilus influenzae RD (Q57399)
Vigonsky, E.; Ovcharenko, E.; Lewinson, O.
Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins
Proc. Natl. Acad. Sci. USA
110
5440-5445
2013
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O30144), Haemophilus influenzae, Haemophilus influenzae (Q4QJQ0)
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