ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
6-259
3.35e-157
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
The actual alignment was detected with superfamily member cd24103:
Pssm-ID: 483947 Cd Length: 255 Bit Score: 437.23 E-value: 3.35e-157
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ...
6-259
3.35e-157
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily includes a group of proteins such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). HgdC (EC 3.6.1.-), also called (R)-2-hydroxyglutaryl-CoA dehydratase activase, (R)-2-hydroxyglutaryl-CoA dehydratase (component A), ATP-coupled electron transfer protein HgdC, or activator of (R)-2-hydroxyglutaryl-CoA dehydratase, is involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity. Its role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic amounts of ATP and substoichiometric amounts of HgdC (CompA) to be functional. HadI is involved in the reductive branch of L-leucine fermentation. It is required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. FldI (EC 3.6.1.-), also called initiator of phenyllactate dehydratase, is involved in the fermentation of L-phenylalanine via a Stickland reaction. It is required for the activation of the (R)-phenyllactate dehydratase complex FldABC. Only in the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer. LcdC, also called lactoyl-CoA dehydratase component E I, is required for the activation of lactoyl-CoA dehydratase. HadI, FldI and LcdC are extremely sensitive towards oxygen.
Pssm-ID: 466953 Cd Length: 255 Bit Score: 437.23 E-value: 3.35e-157
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
5-253
1.90e-89
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.
Pssm-ID: 129344 Cd Length: 248 Bit Score: 265.50 E-value: 1.90e-89
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
7-255
2.87e-76
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 232.63 E-value: 2.87e-76
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ...
6-259
3.35e-157
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily includes a group of proteins such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). HgdC (EC 3.6.1.-), also called (R)-2-hydroxyglutaryl-CoA dehydratase activase, (R)-2-hydroxyglutaryl-CoA dehydratase (component A), ATP-coupled electron transfer protein HgdC, or activator of (R)-2-hydroxyglutaryl-CoA dehydratase, is involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity. Its role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic amounts of ATP and substoichiometric amounts of HgdC (CompA) to be functional. HadI is involved in the reductive branch of L-leucine fermentation. It is required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. FldI (EC 3.6.1.-), also called initiator of phenyllactate dehydratase, is involved in the fermentation of L-phenylalanine via a Stickland reaction. It is required for the activation of the (R)-phenyllactate dehydratase complex FldABC. Only in the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer. LcdC, also called lactoyl-CoA dehydratase component E I, is required for the activation of lactoyl-CoA dehydratase. HadI, FldI and LcdC are extremely sensitive towards oxygen.
Pssm-ID: 466953 Cd Length: 255 Bit Score: 437.23 E-value: 3.35e-157
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ...
6-254
1.58e-128
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 364.55 E-value: 1.58e-128
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ...
6-254
5.71e-106
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ATPase family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL, Methanocaldococcus jannaschii protein MJ0800, and Aquifex aeolicus hypothetical protein O66634, are also includes in this family. The members of the O66634-like group contain two copies of the BcrAD/BadFG-like region suggesting that they may structurally dimerize. The BcrAD/BadFG-like ATPase family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466852 [Multi-domain] Cd Length: 255 Bit Score: 307.44 E-value: 5.71e-106
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ...
7-255
2.54e-98
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.
Pssm-ID: 466954 Cd Length: 253 Bit Score: 288.04 E-value: 2.54e-98
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
7-254
8.46e-95
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YjiL, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.
Pssm-ID: 466959 [Multi-domain] Cd Length: 243 Bit Score: 278.69 E-value: 8.46e-95
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ...
6-255
2.11e-93
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar proteins; bzd-type benzoyl-CoA reductase BzdP is encoded by the gene bzdP from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdP may function the same as the D subunit of benzoyl-CoA reductase BcrD from Thauera aromatica and benzoyl-CoA reductase BadG from Rhodopseudomonas palustris.
Pssm-ID: 466957 [Multi-domain] Cd Length: 250 Bit Score: 275.19 E-value: 2.11e-93
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ...
6-255
6.98e-90
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and similar proteins; bzd-type benzoyl-CoA reductase BzdQ is encoded by the gene bzdQ from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdQ may function the same as the A subunit of benzoyl-CoA reductase BcrA from Thauera aromatica and benzoyl-CoA reductase BadF from Rhodopseudomonas palustris.
Pssm-ID: 466956 Cd Length: 253 Bit Score: 266.39 E-value: 6.98e-90
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
5-253
1.90e-89
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.
Pssm-ID: 129344 Cd Length: 248 Bit Score: 265.50 E-value: 1.90e-89
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ...
6-258
3.72e-84
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar proteins; benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit D of benzoyl-CoA reductase.
Pssm-ID: 466955 Cd Length: 256 Bit Score: 252.12 E-value: 3.72e-84
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
7-255
2.87e-76
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 232.63 E-value: 2.87e-76
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ...
7-260
3.62e-64
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the second copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466885 Cd Length: 258 Bit Score: 201.22 E-value: 3.62e-64
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ...
6-255
1.14e-55
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466884 [Multi-domain] Cd Length: 258 Bit Score: 179.32 E-value: 1.14e-55
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ...
6-255
2.99e-47
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ0800, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.
Pssm-ID: 466958 Cd Length: 259 Bit Score: 158.00 E-value: 2.99e-47
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
