CO dehydrogenase/CO-methylating acetyl-CoA synthase complex, beta subunit; Nomenclature ...
2-462
0e+00
CO dehydrogenase/CO-methylating acetyl-CoA synthase complex, beta subunit; Nomenclature follows the description for Methanosarcina thermophila. The CO-methylating acetyl-CoA synthase is considered the defining enzyme of the Wood-Ljungdahl pathway, used for acetate catabolism by sulfate reducing bacteria but for acetate biosynthesis by acetogenic bacteria such as oorella thermoacetica (f. Clostridium thermoaceticum). [Energy metabolism, Chemoautotrophy]
Pssm-ID: 129416 Cd Length: 458 Bit Score: 611.86 E-value: 0e+00
acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Members of this family have both ...
5-397
0e+00
acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Members of this family have both alpha and beta regions. Proteins scoring between 400 and 800 have only the C-terminal (beta) region.
Pssm-ID: 468724 [Multi-domain] Cd Length: 707 Bit Score: 544.86 E-value: 0e+00
ACS/CODH beta subunit C-terminal; Acetyl-CoA synthase/CO dehydrogenase (ACS/CODH) is a ...
168-396
1.26e-100
ACS/CODH beta subunit C-terminal; Acetyl-CoA synthase/CO dehydrogenase (ACS/CODH) is a bifunctional enzyme that catalyzes the reversible reduction of CO2 to CO (CODH activity, the beta subunit) and the synthesis or degradation of acetyl-CoA (catalyzed by ACS, the alpha subunit). CODH contains the B-, C-, and D-clusters. This domain represents the middle and C-terminal regions of CODH which have an alpha/beta Rossmann-like fold and are the contribute ligands to the active site C-cluster. The C-cluster generates CO from CO2 and contains one Ni atom, four Fe atoms, and five labile sulfur atoms, arranged as an asymmetrical heteronuclear [Ni-4Fe-5S] cluster.
Pssm-ID: 466082 Cd Length: 245 Bit Score: 301.39 E-value: 1.26e-100
CO dehydrogenase/CO-methylating acetyl-CoA synthase complex, beta subunit; Nomenclature ...
2-462
0e+00
CO dehydrogenase/CO-methylating acetyl-CoA synthase complex, beta subunit; Nomenclature follows the description for Methanosarcina thermophila. The CO-methylating acetyl-CoA synthase is considered the defining enzyme of the Wood-Ljungdahl pathway, used for acetate catabolism by sulfate reducing bacteria but for acetate biosynthesis by acetogenic bacteria such as oorella thermoacetica (f. Clostridium thermoaceticum). [Energy metabolism, Chemoautotrophy]
Pssm-ID: 129416 Cd Length: 458 Bit Score: 611.86 E-value: 0e+00
acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Members of this family have both ...
5-397
0e+00
acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Members of this family have both alpha and beta regions. Proteins scoring between 400 and 800 have only the C-terminal (beta) region.
Pssm-ID: 468724 [Multi-domain] Cd Length: 707 Bit Score: 544.86 E-value: 0e+00
ACS/CODH beta subunit C-terminal; Acetyl-CoA synthase/CO dehydrogenase (ACS/CODH) is a ...
168-396
1.26e-100
ACS/CODH beta subunit C-terminal; Acetyl-CoA synthase/CO dehydrogenase (ACS/CODH) is a bifunctional enzyme that catalyzes the reversible reduction of CO2 to CO (CODH activity, the beta subunit) and the synthesis or degradation of acetyl-CoA (catalyzed by ACS, the alpha subunit). CODH contains the B-, C-, and D-clusters. This domain represents the middle and C-terminal regions of CODH which have an alpha/beta Rossmann-like fold and are the contribute ligands to the active site C-cluster. The C-cluster generates CO from CO2 and contains one Ni atom, four Fe atoms, and five labile sulfur atoms, arranged as an asymmetrical heteronuclear [Ni-4Fe-5S] cluster.
Pssm-ID: 466082 Cd Length: 245 Bit Score: 301.39 E-value: 1.26e-100
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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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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if a domain or superfamily has been annotated with functional sites (conserved features),
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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
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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
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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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