MULTISPECIES: substrate-binding domain-containing protein [unclassified Pseudomonas]
Protein Classification
molybdate ABC transporter substrate-binding protein; substrate-binding domain-containing protein( domain architecture ID 12147048)
molybdate ABC transporter substrate-binding protein functions as the primary receptor for the active transport of molybdate in an ATP-dependent manner; substrate-binding domain-containing protein similar to Pseudomonas sp. aconitate isomerase, which is involved in assimilation of trans-aconitic acid
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| SBP_bac_11 | pfam13531 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
26-246 | 2.51e-32 | ||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. : Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 117.75 E-value: 2.51e-32
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| Name | Accession | Description | Interval | E-value | |||||
| SBP_bac_11 | pfam13531 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
26-246 | 2.51e-32 | |||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 117.75 E-value: 2.51e-32
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| ModA | COG0725 | ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ... |
8-251 | 1.61e-26 | |||||
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440489 [Multi-domain] Cd Length: 253 Bit Score: 103.41 E-value: 1.61e-26
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| PBP2_ModA_like | cd00993 | Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ... |
24-239 | 9.29e-16 | |||||
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein fold; Molybdate binding domain ModA. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has revealed a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270215 [Multi-domain] Cd Length: 225 Bit Score: 73.91 E-value: 9.29e-16
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| modA | TIGR01256 | molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ... |
33-246 | 9.62e-08 | |||||
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. [Transport and binding proteins, Anions] Pssm-ID: 273526 [Multi-domain] Cd Length: 216 Bit Score: 51.26 E-value: 9.62e-08
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| PRK11622 | PRK11622 | ABC transporter substrate-binding protein; |
200-239 | 1.46e-04 | |||||
ABC transporter substrate-binding protein; Pssm-ID: 183238 [Multi-domain] Cd Length: 401 Bit Score: 42.25 E-value: 1.46e-04
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| Name | Accession | Description | Interval | E-value | |||||
| SBP_bac_11 | pfam13531 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
26-246 | 2.51e-32 | |||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 117.75 E-value: 2.51e-32
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| ModA | COG0725 | ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ... |
8-251 | 1.61e-26 | |||||
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440489 [Multi-domain] Cd Length: 253 Bit Score: 103.41 E-value: 1.61e-26
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| PBP2_ModA_like | cd00993 | Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ... |
24-239 | 9.29e-16 | |||||
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein fold; Molybdate binding domain ModA. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has revealed a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270215 [Multi-domain] Cd Length: 225 Bit Score: 73.91 E-value: 9.29e-16
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| PBP2_ModA_WtpA | cd13540 | Substrate binding domain of ModA/WtpA from Pyrococcus furiosus and its closest homologs;the ... |
24-248 | 1.68e-10 | |||||
Substrate binding domain of ModA/WtpA from Pyrococcus furiosus and its closest homologs;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270258 [Multi-domain] Cd Length: 263 Bit Score: 59.62 E-value: 1.68e-10
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| modA | TIGR01256 | molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ... |
33-246 | 9.62e-08 | |||||
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. [Transport and binding proteins, Anions] Pssm-ID: 273526 [Multi-domain] Cd Length: 216 Bit Score: 51.26 E-value: 9.62e-08
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| PBP2_YvgL_like | cd13537 | Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ... |
88-246 | 1.24e-05 | |||||
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. ModA proteins serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate and tungstate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270255 [Multi-domain] Cd Length: 225 Bit Score: 44.97 E-value: 1.24e-05
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| PBP2_ModA_like_1 | cd13538 | Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ... |
24-246 | 1.38e-05 | |||||
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270256 [Multi-domain] Cd Length: 230 Bit Score: 44.98 E-value: 1.38e-05
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| PRK11622 | PRK11622 | ABC transporter substrate-binding protein; |
200-239 | 1.46e-04 | |||||
ABC transporter substrate-binding protein; Pssm-ID: 183238 [Multi-domain] Cd Length: 401 Bit Score: 42.25 E-value: 1.46e-04
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| PBP2_EcModA | cd13536 | Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 ... |
40-241 | 1.83e-04 | |||||
Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270254 [Multi-domain] Cd Length: 227 Bit Score: 41.63 E-value: 1.83e-04
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| PBP2_BitB | cd13546 | Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
148-245 | 2.07e-04 | |||||
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270264 [Multi-domain] Cd Length: 258 Bit Score: 41.47 E-value: 2.07e-04
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| PBP2_AvModA | cd13539 | Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the ... |
24-248 | 1.83e-03 | |||||
Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate is where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270257 [Multi-domain] Cd Length: 226 Bit Score: 38.70 E-value: 1.83e-03
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| AfuA | COG1840 | ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
171-239 | 2.10e-03 | |||||
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 38.76 E-value: 2.10e-03
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