alpha-acetolactate decarboxylase; alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5) converts acetolactate ((2S)-2-hydroxy-2-methyl-3-oxobutanoate) into acetoin ((3R)-3-hydroxybutan-2-one) and CO(2). Acetoin may be secreted by the cells, perhaps in order to control the internal pH. AldB may function as a regulator in valine and leucine biosynthesis and in catalyzing the second step of the 2,3-butanediol pathway. The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxxH motif (x could be any residue) that coordinates a zinc ion.
Pssm-ID: 341211 Cd Length: 232 Bit Score: 334.82 E-value: 3.50e-117
alpha-acetolactate decarboxylase; Puruvate can be fermented to 2,3-butanediol. It is first ...
28-258
1.73e-103
alpha-acetolactate decarboxylase; Puruvate can be fermented to 2,3-butanediol. It is first converted to alpha-acetolactate by alpha-acetolactate synthase, then decarboxylated to acetoin by this enzyme. Acetoin can be reduced in some species to 2,3-butanediol by acetoin reductase. [Energy metabolism, Fermentation]
Pssm-ID: 273524 Cd Length: 232 Bit Score: 300.11 E-value: 1.73e-103
alpha-acetolactate decarboxylase; alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5) converts acetolactate ((2S)-2-hydroxy-2-methyl-3-oxobutanoate) into acetoin ((3R)-3-hydroxybutan-2-one) and CO(2). Acetoin may be secreted by the cells, perhaps in order to control the internal pH. AldB may function as a regulator in valine and leucine biosynthesis and in catalyzing the second step of the 2,3-butanediol pathway. The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxxH motif (x could be any residue) that coordinates a zinc ion.
Pssm-ID: 341211 Cd Length: 232 Bit Score: 334.82 E-value: 3.50e-117
alpha-acetolactate decarboxylase; Puruvate can be fermented to 2,3-butanediol. It is first ...
28-258
1.73e-103
alpha-acetolactate decarboxylase; Puruvate can be fermented to 2,3-butanediol. It is first converted to alpha-acetolactate by alpha-acetolactate synthase, then decarboxylated to acetoin by this enzyme. Acetoin can be reduced in some species to 2,3-butanediol by acetoin reductase. [Energy metabolism, Fermentation]
Pssm-ID: 273524 Cd Length: 232 Bit Score: 300.11 E-value: 1.73e-103
proteins similar to alpha-acetolactate dehydrogenase; The structure of this domain displays an ...
28-234
1.15e-93
proteins similar to alpha-acetolactate dehydrogenase; The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an H(x)H(x)nH motif (x could be any residue, n could be 9 or 10) that coordinates a zinc ion. The proteins are homologous to bacterial alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5), which converts acetolactate into acetoin.
Pssm-ID: 341209 Cd Length: 209 Bit Score: 274.34 E-value: 1.15e-93
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.
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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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Others (non-specific hits) and
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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)
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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
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