Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy ...
1-298
2.80e-154
Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy production and conversion]; Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain is part of the Pathway/BioSystem: TCA cycle
:
Pssm-ID: 441554 Cd Length: 289 Bit Score: 441.05 E-value: 2.80e-154
Fumarase C-terminus; This family consists of the C terminal region of several bacterial ...
289-491
1.80e-124
Fumarase C-terminus; This family consists of the C terminal region of several bacterial fumarate hydratase proteins (FumA and FumB). Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth.
:
Pssm-ID: 461714 [Multi-domain] Cd Length: 204 Bit Score: 361.79 E-value: 1.80e-124
Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy ...
1-298
2.80e-154
Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy production and conversion]; Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 441554 Cd Length: 289 Bit Score: 441.05 E-value: 2.80e-154
Fumarate hydratase (Fumerase); This family consists of several bacterial fumarate hydratase ...
10-283
1.77e-133
Fumarate hydratase (Fumerase); This family consists of several bacterial fumarate hydratase proteins FumA and FumB. Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth. Three fumarases, FumA, FumB, and FumC, have been reported in E. coli. fumA and fumB genes are homologous and encode products of identical sizes which form thermolabile dimers of Mr 120,000. FumA and FumB are class I enzymes and are members of the iron-dependent hydrolases, which include aconitase and malate hydratase. The active FumA contains a 4Fe-4S centre, and it can be inactivated upon oxidation to give a 3Fe-4S centre.
Pssm-ID: 461713 Cd Length: 267 Bit Score: 387.15 E-value: 1.77e-133
Fumarase C-terminus; This family consists of the C terminal region of several bacterial ...
289-491
1.80e-124
Fumarase C-terminus; This family consists of the C terminal region of several bacterial fumarate hydratase proteins (FumA and FumB). Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth.
Pssm-ID: 461714 [Multi-domain] Cd Length: 204 Bit Score: 361.79 E-value: 1.80e-124
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy ...
316-503
3.34e-105
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy production and conversion]; Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 441443 Cd Length: 190 Bit Score: 312.04 E-value: 3.34e-105
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, alpha region; A number of Fe-S ...
11-282
4.13e-61
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, alpha region; A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase alpha chain and the N-terminal region of the class I fumarase (where the C-terminal region is homologous to the tartrate dehydratase beta chain). The activity of archaeal proteins in this subfamily has not been established.
Pssm-ID: 273234 Cd Length: 273 Bit Score: 201.54 E-value: 4.13e-61
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S ...
325-487
1.55e-50
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase beta chain and the C-terminal region of the class I fumarase (where the N-terminal region is homologous to the tartrate dehydratase alpha chain). The activity of archaeal proteins in this subfamily has not been established.
Pssm-ID: 129806 Cd Length: 168 Bit Score: 170.31 E-value: 1.55e-50
Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy ...
1-298
2.80e-154
Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy production and conversion]; Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 441554 Cd Length: 289 Bit Score: 441.05 E-value: 2.80e-154
Fumarate hydratase (Fumerase); This family consists of several bacterial fumarate hydratase ...
10-283
1.77e-133
Fumarate hydratase (Fumerase); This family consists of several bacterial fumarate hydratase proteins FumA and FumB. Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth. Three fumarases, FumA, FumB, and FumC, have been reported in E. coli. fumA and fumB genes are homologous and encode products of identical sizes which form thermolabile dimers of Mr 120,000. FumA and FumB are class I enzymes and are members of the iron-dependent hydrolases, which include aconitase and malate hydratase. The active FumA contains a 4Fe-4S centre, and it can be inactivated upon oxidation to give a 3Fe-4S centre.
Pssm-ID: 461713 Cd Length: 267 Bit Score: 387.15 E-value: 1.77e-133
Fumarase C-terminus; This family consists of the C terminal region of several bacterial ...
289-491
1.80e-124
Fumarase C-terminus; This family consists of the C terminal region of several bacterial fumarate hydratase proteins (FumA and FumB). Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth.
Pssm-ID: 461714 [Multi-domain] Cd Length: 204 Bit Score: 361.79 E-value: 1.80e-124
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy ...
316-503
3.34e-105
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy production and conversion]; Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 441443 Cd Length: 190 Bit Score: 312.04 E-value: 3.34e-105
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, alpha region; A number of Fe-S ...
11-282
4.13e-61
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, alpha region; A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase alpha chain and the N-terminal region of the class I fumarase (where the C-terminal region is homologous to the tartrate dehydratase beta chain). The activity of archaeal proteins in this subfamily has not been established.
Pssm-ID: 273234 Cd Length: 273 Bit Score: 201.54 E-value: 4.13e-61
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S ...
325-487
1.55e-50
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase beta chain and the C-terminal region of the class I fumarase (where the N-terminal region is homologous to the tartrate dehydratase alpha chain). The activity of archaeal proteins in this subfamily has not been established.
Pssm-ID: 129806 Cd Length: 168 Bit Score: 170.31 E-value: 1.55e-50
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.
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of your query sequence and the protein sequences used to curate the domain model,
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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.
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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
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Domains are color coded according to superfamilies
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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
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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
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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
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