nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
9-298
0e+00
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase (EcGppA) and similar proteins; EcGppA (EC 3.6.1.40), also called guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase, or pppGpp-5'-phosphohydrolase, catalyzes the conversion of guanosine pentaphosphate (pppGpp) to guanosine tetraphosphate (ppGpp). pppGpp is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. EcGppA also has exopolyphosphatase activity, catalyzing the release of orthophosphate by processive hydrolysis of the phosphoanyhydride bonds of polyphosphate chains. Unlike other PPX/GppA family members containing one PPX/GppA homolog, E. coli possesses two homologs, EcGppA and EcPPX, which are indistinguishable in their domain arrangement.
Pssm-ID: 466967 [Multi-domain] Cd Length: 290 Bit Score: 558.20 E-value: 0e+00
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
21-301
4.85e-122
Ppx/GppA phosphatase family; This family consists of the N-terminal region of exopolyphosphatase (Ppx) EC:3.6.1.11 and guanosine pentaphosphate phospho-hydrolase (GppA) EC:3.6.1.40.
Pssm-ID: 396889 [Multi-domain] Cd Length: 285 Bit Score: 358.17 E-value: 4.85e-122
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
7-300
4.05e-107
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274735 [Multi-domain] Cd Length: 300 Bit Score: 320.65 E-value: 4.05e-107
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase ...
9-298
0e+00
nucleotide-binding domain (NBD) of Escherichia coli guanosine pentaphosphate phosphohydrolase (EcGppA) and similar proteins; EcGppA (EC 3.6.1.40), also called guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase, or pppGpp-5'-phosphohydrolase, catalyzes the conversion of guanosine pentaphosphate (pppGpp) to guanosine tetraphosphate (ppGpp). pppGpp is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. EcGppA also has exopolyphosphatase activity, catalyzing the release of orthophosphate by processive hydrolysis of the phosphoanyhydride bonds of polyphosphate chains. Unlike other PPX/GppA family members containing one PPX/GppA homolog, E. coli possesses two homologs, EcGppA and EcPPX, which are indistinguishable in their domain arrangement.
Pssm-ID: 466967 [Multi-domain] Cd Length: 290 Bit Score: 558.20 E-value: 0e+00
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine ...
9-297
1.06e-142
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX), guanosine pentaphosphate phosphohydrolase (EcGppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to Escherichia coli exopolyphosphatase (EcPPX) and guanosine pentaphosphate phosphohydrolase (EcGppA). Unlike other PPX/GppA family members containing one PPX/GppA homolog, E. coli possesses two homologs, EcGppA and EcPPX.
Pssm-ID: 466903 [Multi-domain] Cd Length: 292 Bit Score: 411.16 E-value: 1.06e-142
Ppx/GppA phosphatase family; This family consists of the N-terminal region of ...
21-301
4.85e-122
Ppx/GppA phosphatase family; This family consists of the N-terminal region of exopolyphosphatase (Ppx) EC:3.6.1.11 and guanosine pentaphosphate phospho-hydrolase (GppA) EC:3.6.1.40.
Pssm-ID: 396889 [Multi-domain] Cd Length: 285 Bit Score: 358.17 E-value: 4.85e-122
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar ...
9-299
2.35e-111
nucleotide-binding domain (NBD) of Escherichia coli exopolyphosphatase (EcPPX) and similar proteins; EcPPX (EC 3.6.1.11), also called exopolyPase, or metaphosphatase, mediates the metabolism of cellular inorganic polyphosphate (polyP). It catalyzes degradation of polyP and releases orthophosphate processively from the ends of the polyP chain. It has a strong preference for long-chain polyphosphates and has only weak affinity for smaller size polyP of about 15 residues. Unlike other PPX/GppA family members containing one PPX/GppA homolog, E. coli possesses two homologs, EcGppA and EcPPX, which are indistinguishable in their domain arrangement.
Pssm-ID: 466966 [Multi-domain] Cd Length: 299 Bit Score: 331.72 E-value: 2.35e-111
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) ...
7-300
4.05e-107
exopolyphosphatase; It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274735 [Multi-domain] Cd Length: 300 Bit Score: 320.65 E-value: 4.05e-107
nucleotide-binding domain (NBD) of Aquifex aeolicus PPX/GppA, Mycobacterium tuberculosis PPX2, Fusobacterium nucleatum AroB, and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds to a group of proteins similar to Aquifex aeolicus exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (AaPPX/GppA), Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2), Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB) and similar proteins.
Pssm-ID: 466904 [Multi-domain] Cd Length: 296 Bit Score: 227.36 E-value: 8.67e-71
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ...
9-297
4.93e-70
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466856 [Multi-domain] Cd Length: 294 Bit Score: 225.11 E-value: 4.93e-70
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
8-300
1.15e-56
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (HpPPX/GppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to Helicobacter pylori PPX/GppA (HpPPX/GppA). HpPPX/GppA is phylogenetically distant from the Escherichia coli homologs. Unlike E. coli that possesses two homologs, EcGppA and EcPPX, H. pylori encodes only one PPX/GppA homolog, HpPPX/GppA. As such, HpPPX/GppA may play important roles in the homeostasis of both (p)ppGpp and PolyP.
Pssm-ID: 466902 [Multi-domain] Cd Length: 298 Bit Score: 190.39 E-value: 1.15e-56
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) ...
9-296
4.05e-49
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 2 (MtPPX2) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Mycobacterium tuberculosis encodes two PPX/GppA homologues, Rv0496 (MtPPX1) and Rv1026 (MtPPX2), which are analogous to the Escherichia coli PPX and GppA enzymes. MtPPX1 functions as an exopolyphosphatase, showing a distinct preference for relatively short-chain poly-P substrates. The exopolyphosphatase activities of MtPPX1 are inhibited by pppGpp. In contrast, MtPPX2 has no detectable exopolyphosphatase activities. Neither MtPPX1 nor MtPPX2 can hydrolyze pppGpp to ppGpp, which is a reaction catalyzed by E. coli PPX and GppA enzymes. Both the MtPPX1 and MtPPX2 proteins have modest ATPase and to a lesser extent ADPase activities. The family corresponds a group of proteins similar to MtPPX2.
Pssm-ID: 466969 [Multi-domain] Cd Length: 298 Bit Score: 170.52 E-value: 4.05e-49
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) ...
9-296
1.08e-46
nucleotide-binding domain (NBD) of Mycobacterium tuberculosis exopolyphosphatase 1 (MtPPX1) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Mycobacterium tuberculosis encodes two PPX/GppA homologues, Rv0496 (MtPPX1) and Rv1026 (MtPPX2), which are analogous to the Escherichia coli PPX and GppA enzymes. MtPPX1 functions as an exopolyphosphatase, showing a distinct preference for relatively short-chain poly-P substrates. The exopolyphosphatase activities of MtPPX1 are inhibited by pppGpp. In contrast, MtPPX2 has no detectable exopolyphosphatase activities. Neither MtPPX1 nor MtPPX2 can hydrolyze pppGpp to ppGpp, which is a reaction catalyzed by E. coli PPX and GppA enzymes. Both the MtPPX1 and MtPPX2 proteins have modest ATPase and to a lesser extent ADPase activities. The family corresponds a group of proteins similar to MtPPX1.
Pssm-ID: 466906 [Multi-domain] Cd Length: 302 Bit Score: 164.32 E-value: 1.08e-46
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and ...
9-297
1.21e-46
nucleotide-binding domain (NBD) of Cytophaga hutchinsonii exopolyphosphatase (ChPPX) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to uncharacterized Cytophaga hutchinsonii exopolyphosphatase (ChPPX).
Pssm-ID: 466905 [Multi-domain] Cd Length: 300 Bit Score: 163.89 E-value: 1.21e-46
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate ...
9-297
1.26e-37
nucleotide-binding domain (NBD) of Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB) and similar proteins; The family includes a group of PPX/GppA family proteins similar to Fusobacterium nucleatum bifunctional 3-dehydroquinate synthase/phosphatase (AroB; EC 4.2.3.4/EC 3.6.1.-). AroB contains 3-dehydroquinate synthase and an unknown phosphatase. 3-dehydroquinate synthase catalyzes the second step in the shikimate pathway, which is essential to produce aromatic amino acids in bacteria, plants, and fungi, but not mammals.
Pssm-ID: 466970 [Multi-domain] Cd Length: 297 Bit Score: 139.76 E-value: 1.26e-37
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine ...
9-296
1.84e-28
nucleotide-binding domain (NBD) of Aquifex aeolicus exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (AaPPX/GppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds to a group of proteins similar to Aquifex aeolicus PPX/GppA (AaPPX/GppA). AaPPX/GppA is phylogenetically distant from the Escherichia coli homologs. Unlike E. coli that possesses two homologs, EcGppA and EcPPX, A. aeolicus encodes only one PPX/GppA homolog, AaPPX/GppA. As such, AaPPX/GppA may play important roles in the homeostasis of both (p)ppGpp and PolyP.
Pssm-ID: 466968 [Multi-domain] Cd Length: 293 Bit Score: 114.48 E-value: 1.84e-28
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
(CDART).
Modify your query to search against a different database and/or use advanced search options