Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
28-443
0e+00
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture.
:
Pssm-ID: 153082 Cd Length: 417 Bit Score: 644.16 E-value: 0e+00
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
28-443
0e+00
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture.
Pssm-ID: 153082 Cd Length: 417 Bit Score: 644.16 E-value: 0e+00
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; ...
27-439
0e+00
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; Hydroxymethylglutaryl-CoA reductase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440869 Cd Length: 409 Bit Score: 573.63 E-value: 0e+00
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
34-406
7.47e-127
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of HMG-CoA to mevalonate, which is the rate-limiting step in the synthesis of isoprenoids like cholesterol. Probably because of the critical role of this enzyme in cholesterol homeostasis, mammalian HMG-CoA reductase is heavily regulated at the transcriptional, translational, and post-translational levels.
Pssm-ID: 459786 Cd Length: 368 Bit Score: 372.17 E-value: 7.47e-127
hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of ...
25-406
8.19e-123
hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of hydroxymethylglutaryl-CoA reductase are NADP-dependent (EC 1.1.1.34) from eukaryotes and archaea, involved in the biosynthesis of mevalonate from 3-hydroxy-3-methylglutaryl-CoA. This model, in contrast, is built from the two examples in completed genomes of sequences closely related to the degradative, NAD-dependent hydroxymethylglutaryl-CoA reductase of Pseudomonas mevalonii, a bacterium that can use mevalonate as its sole carbon source. [Energy metabolism, Other]
Pssm-ID: 129623 Cd Length: 393 Bit Score: 362.81 E-value: 8.19e-123
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
28-443
0e+00
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture.
Pssm-ID: 153082 Cd Length: 417 Bit Score: 644.16 E-value: 0e+00
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; ...
27-439
0e+00
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; Hydroxymethylglutaryl-CoA reductase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440869 Cd Length: 409 Bit Score: 573.63 E-value: 0e+00
Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A ...
28-406
1.19e-128
Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) is a tightly regulated enzyme, which catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals, this is the rate limiting committed step in cholesterol biosynthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. There are two classes of HMGR: class I enzymes which are found predominantly in eukaryotes and contain N-terminal membrane regions and class II enzymes which are found primarily in prokaryotes and are soluble as they lack the membrane region. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture. While the prokaryotic enzyme is a homodimer, the eukaryotic enzyme is a homotetramer.
Pssm-ID: 153080 Cd Length: 376 Bit Score: 377.02 E-value: 1.19e-128
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
34-406
7.47e-127
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of HMG-CoA to mevalonate, which is the rate-limiting step in the synthesis of isoprenoids like cholesterol. Probably because of the critical role of this enzyme in cholesterol homeostasis, mammalian HMG-CoA reductase is heavily regulated at the transcriptional, translational, and post-translational levels.
Pssm-ID: 459786 Cd Length: 368 Bit Score: 372.17 E-value: 7.47e-127
hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of ...
25-406
8.19e-123
hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of hydroxymethylglutaryl-CoA reductase are NADP-dependent (EC 1.1.1.34) from eukaryotes and archaea, involved in the biosynthesis of mevalonate from 3-hydroxy-3-methylglutaryl-CoA. This model, in contrast, is built from the two examples in completed genomes of sequences closely related to the degradative, NAD-dependent hydroxymethylglutaryl-CoA reductase of Pseudomonas mevalonii, a bacterium that can use mevalonate as its sole carbon source. [Energy metabolism, Other]
Pssm-ID: 129623 Cd Length: 393 Bit Score: 362.81 E-value: 8.19e-123
Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
65-404
6.71e-10
Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class I enzyme, homotetramer. Catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals this is the rate limiting committed step in cholesterol biosynthesis. Class I enzymes are found predominantly in eukaryotes and contain N-terminal membrane regions. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture.
Pssm-ID: 153081 Cd Length: 403 Bit Score: 60.64 E-value: 6.71e-10
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
