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Literature summary for 7.3.2.5 extracted from
- Bacterial transport of sulfate, molybdate, and related oxyanions (2011), Biometals, 24, 687-707.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds | Escherichia coli |
| ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds | Azotobacter vinelandii |
| ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds | Xanthomonas axonopodis |
| ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds | Archaeoglobus fulgidus |
| ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds | Pyrococcus horikoshii |
| ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds | Methanosarcina acetivorans |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | ModB and ModC, ModB possesses six transmembrane domains | Escherichia coli | 16020 | - |
| membrane | ModB and ModC, ModB possesses six transmembrane domains | Azotobacter vinelandii | 16020 | - |
| membrane | ModB and ModC, ModB possesses six transmembrane domains | Xanthomonas axonopodis | 16020 | - |
| membrane | ModB possesses six transmembrane domains | Archaeoglobus fulgidus | 16020 | - |
| membrane | ModB possesses six transmembrane domains | Methanosarcina acetivorans | 16020 | - |
| periplasm | ModA | Escherichia coli | - |
- |
| periplasm | ModA | Azotobacter vinelandii | - |
- |
| periplasm | ModA | Xanthomonas axonopodis | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + molybdate/out | Escherichia coli | - |
ADP + phosphate + molybdate/in | - |
? |  |
| ATP + H2O + molybdate/out | Rhodobacter capsulatus | - |
ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | Azotobacter vinelandii | - |
ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | Archaeoglobus fulgidus | - |
ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | Pyrococcus horikoshii | - |
ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | Methanosarcina acetivorans | - |
ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | Xanthomonas axonopodis | - |
ADP + phosphate + molybdate/in | - |
? | |
| additional information | Azotobacter vinelandii | ModABC can also transport tungstate | ? | - |
? | |
| additional information | Escherichia coli | ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite | ? | - |
? | |
| additional information | Xanthomonas axonopodis | ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite | ? | - |
? | |
| additional information | Archaeoglobus fulgidus | ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate | ? | - |
? | |
| additional information | Methanosarcina acetivorans | ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate, WtpABC transports tungstate and molybdate in Pyrococcus furiosus | ? | - |
? | |
| additional information | Rhodobacter capsulatus | PerO transports molybdate, sulfate, tungstate, and vanadate in Rhodobacter capsulatus functioning as a general oxyanion transporter | ? | - |
? | |
| additional information | Pyrococcus horikoshii | WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | - |
- |
- |
| Azotobacter vinelandii | - |
modABC operon | - |
| Escherichia coli | - |
ModABC transporter is encoded by the modABC operon, gene modA encodes the molybdate-binding protein ModA, ModC is encoded by the modC gene and is the ATPase subunit | - |
| Methanosarcina acetivorans | - |
possesses ModA and WtpA transporters | - |
| Pyrococcus horikoshii | - |
- |
- |
| Rhodobacter capsulatus | - |
modABC operon | - |
| Xanthomonas axonopodis | - |
pv. citri, modABC operon | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + molybdate/out | - |
Escherichia coli | ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | - |
Rhodobacter capsulatus | ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | - |
Azotobacter vinelandii | ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | - |
Archaeoglobus fulgidus | ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | - |
Pyrococcus horikoshii | ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | - |
Methanosarcina acetivorans | ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | - |
Xanthomonas axonopodis | ADP + phosphate + molybdate/in | - |
? | |
| ATP + H2O + molybdate/out | two ATP per imported molybdate | Archaeoglobus fulgidus | ADP + phosphate + molybdate/in | - |
? | |
| additional information | ModABC can also transport tungstate | Azotobacter vinelandii | ? | - |
? | |
| additional information | ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite | Escherichia coli | ? | - |
? | |
| additional information | ModABC can also transport tungstate and sulfate, while the sulfate/thiosulfate permease, CysPTWA belonging to the sulfate/tungstate uptake transporter SulT family, of Escherichia coli can transport sulfate, chromate, molybdate, and selenate, overview. Molybdate can also be taken up by a non-specific low-efficiency anion transport system that requires high molybdate concentrations, and which also transports sulfate, selenate, and selenite | Xanthomonas axonopodis | ? | - |
? | |
| additional information | ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate | Archaeoglobus fulgidus | ? | - |
? | |
| additional information | ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate, WtpABC transports tungstate and molybdate in Pyrococcus furiosus | Methanosarcina acetivorans | ? | - |
? | |
| additional information | PerO transports molybdate, sulfate, tungstate, and vanadate in Rhodobacter capsulatus functioning as a general oxyanion transporter | Rhodobacter capsulatus | ? | - |
? | |
| additional information | WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview | Pyrococcus horikoshii | ? | - |
? | |
| additional information | ModA specifically binds Kd of 290 nM for molybdate and 580 nM for tungstate | Xanthomonas axonopodis | ? | - |
? | |
| additional information | ModA specifically binds molybdate and tungstate | Azotobacter vinelandii | ? | - |
? | |
| additional information | ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate with a Kd of ca. 20 nM. ModE functions as a homodimer and binds two molecules of molybdate with high affinity, Kd = 800 nM | Escherichia coli | ? | - |
? | |
| additional information | WtpABC transports tungstate and molybdate in Pyrococcus furiosus | Pyrococcus horikoshii | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | archaeal ModA proteins possess octahedral coordination | Pyrococcus horikoshii |
| More | archaeal ModA proteins possess octahedral coordination, structure of the ModAB2C2 complex, overview. A single ModA protein with the molybdate oxyanion bound to the external side of a ModB2C2 complex. Molybdate or tungstate oxyanions are bound in a cleft between two lobes in ModA. Both lobes interact with ModB and there are several charged residues localized on the interface | Archaeoglobus fulgidus |
| More | archaeal ModA proteins possess octahedral coordination, structure of the ModABC complex, overview | Methanosarcina acetivorans |
| More | bacterial ModA proteins possess tetrahedral coordination | Escherichia coli |
| More | bacterial ModA proteins possess tetrahedral coordination | Rhodobacter capsulatus |
| More | bacterial ModA proteins possess tetrahedral coordination | Azotobacter vinelandii |
| More | bacterial ModA proteins possess tetrahedral coordination | Xanthomonas axonopodis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ModA/WtpA | - |
Archaeoglobus fulgidus |
| ModA/WtpA | - |
Pyrococcus horikoshii |
| ModA/WtpA | - |
Methanosarcina acetivorans |
| ModABC | - |
Escherichia coli |
| ModABC | - |
Rhodobacter capsulatus |
| ModABC | - |
Azotobacter vinelandii |
| ModABC | - |
Archaeoglobus fulgidus |
| ModABC | - |
Methanosarcina acetivorans |
| ModABC | - |
Xanthomonas axonopodis |
| ModABC transporter | - |
Archaeoglobus fulgidus |
| ModABC transporter | - |
Methanosarcina acetivorans |
| molybdate- or tungstate-binding protein | - |
Archaeoglobus fulgidus |
| molybdate- or tungstate-binding protein | - |
Pyrococcus horikoshii |
| molybdate- or tungstate-binding protein | - |
Methanosarcina acetivorans |
| WtpABC | - |
Pyrococcus horikoshii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | ModABC belongs to the family of molybdate uptake transporters MolT | Escherichia coli |
| evolution | ModABC belongs to the family of molybdate uptake transporters MolT | Azotobacter vinelandii |
| evolution | ModABC belongs to the family of molybdate uptake transporters MolT | Archaeoglobus fulgidus |
| evolution | ModABC belongs to the family of molybdate uptake transporters MolT | Xanthomonas axonopodis |
| evolution | ModABC belongs to the family of molybdate uptake transporters MolT, PerO belongs to the ArsB/NhaD ion transporter family | Rhodobacter capsulatus |
| evolution | WtpABC belongs to the sulfate/tungstate uptake transporter SulT family, overview. ModABC belongs to the family of molybdate uptake transporters MolT | Pyrococcus horikoshii |
| evolution | WtpABC belongs to the sulfate/tungstate uptake transporter SulT family, overview. ModABC belongs to the family of molybdate uptake transporters MolT | Methanosarcina acetivorans |
| physiological function | ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport | Azotobacter vinelandii |
| physiological function | ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport | Archaeoglobus fulgidus |
| physiological function | ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport | Pyrococcus horikoshii |
| physiological function | ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport | Xanthomonas axonopodis |
| physiological function | ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport. ATPase ModC from Methanosarcina acetivorans possesses a regulatory domain | Methanosarcina acetivorans |
| physiological function | ModA is responsible for metal binding, ModB functions as a homodimer to form the channel for molybdate transport, ModC is the ATPase subunit of the ModABC complex that energizes molybdate transport. Regulation of the modABC operon by the molybdate-responsive ModE protein, overview. The active form of ModE, which binds to the modA operator, is the ModE-molybdate complex, interaction between the modA operator and ModE-Mo | Escherichia coli |
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