CO dehydrogenase/CO-methylating acetyl-CoA synthase complex subunit is part of an acetyl-CoA decarbonylase/synthase complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2)
acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Members of this family have both ...
10-734
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.
The actual alignment was detected with superfamily member NF040764:
Pssm-ID: 468724 [Multi-domain] Cd Length: 707 Bit Score: 1227.44 E-value: 0e+00
acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Members of this family have both ...
10-734
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: 1227.44 E-value: 0e+00
ACS/CODH beta subunit C-terminal; Acetyl-CoA synthase/CO dehydrogenase (ACS/CODH) is a ...
491-734
1.38e-162
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: 468.57 E-value: 1.38e-162
CO dehydrogenase/CO-methylating acetyl-CoA synthase complex, beta subunit; Nomenclature ...
325-729
2.64e-135
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: 406.93 E-value: 2.64e-135
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
20-319
3.35e-50
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238898 Cd Length: 287 Bit Score: 177.35 E-value: 3.35e-50
acetyl-CoA decarbonylase/synthase complex subunit alpha/beta; Members of this family have both ...
10-734
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: 1227.44 E-value: 0e+00
ACS/CODH beta subunit C-terminal; Acetyl-CoA synthase/CO dehydrogenase (ACS/CODH) is a ...
491-734
1.38e-162
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: 468.57 E-value: 1.38e-162
CO dehydrogenase/CO-methylating acetyl-CoA synthase complex, beta subunit; Nomenclature ...
325-729
2.64e-135
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: 406.93 E-value: 2.64e-135
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
20-319
3.35e-50
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238898 Cd Length: 287 Bit Score: 177.35 E-value: 3.35e-50
Carbon monoxide dehydrogenase subunit alpha N-terminal domain; Acetyl-coenzyme A (CoA) synthase/carbon monoxide dehydrogenase (ACS/CODH) is a bifunctional enzyme that catalyzes the reversible reduction of CO2 to CO (CODH activity). This entry is for the N-terminal domain found in ACS/CODH subunit alpha.
Pssm-ID: 465793 [Multi-domain] Cd Length: 83 Bit Score: 118.78 E-value: 6.84e-32
The HCP family of iron-sulfur proteins includes hybrid cluster protein (HCP), acetyl-CoA ...
90-286
7.35e-05
The HCP family of iron-sulfur proteins includes hybrid cluster protein (HCP), acetyl-CoA synthase (ACS), and carbon monoxide dehydrogenase (CODH), all of which contain [Fe4-S4] metal clusters at their active sites. These proteins have a conserved alpha-beta rossman fold domain. HCP, formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. Acetyl-CoA synthase (ACS), is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide and CoA.
Pssm-ID: 238330 [Multi-domain] Cd Length: 258 Bit Score: 45.28 E-value: 7.35e-05
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.
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