HAMAP rule MF_01137
General rule information
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Accession | MF_01137 |
Dates | 20-NOV-2003 (Created)
1-JUN-2023 (Last updated, Version 25) |
Name | CdhA |
Scope(s) |
Archaea |
Template(s) | Q08368 (ACDA1_METTE); Q46G04 (ACDA1_METBF); [ Recover all ] |
Triggered by |
HAMAP; MF_01137 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | ACDA |
Protein name | RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha; Short=ACDS complex subunit alpha; EC=1.2.7.4; AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha; Short=ACDS CODH subunit alpha; |
Gene name | Name=cdhA; |
Comments
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case <OC:Methanosarcinaceae> | |
FUNCTION | Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. |
end case | |
case not <OC:Methanosarcinaceae> | |
FUNCTION | Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. |
end case | |
CATALYTIC ACTIVITY | Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA- COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4; |
COFACTOR | Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 7 [4Fe-4S] clusters per heterotetramer.; |
COFACTOR | Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739; Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.; |
case <OC:Methanosarcinaceae> | |
PATHWAY | One-carbon metabolism; methanogenesis from acetate. |
end case | |
SUBUNIT | Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)- (gamma(1)delta(1))(8). |
DOMAIN | Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster. |
SIMILARITY | Belongs to the Ni-containing carbon monoxide dehydrogenase family. |
Keywords
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case <OC:Methanosarcinaceae> | |
Methanogenesis | |
end case | |
Oxidoreductase | |
Metal-binding | |
case <FTGroup:3> | |
Nickel | |
end case | |
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3> or <FTGroup:4> or <FTGroup:5> | |
Iron | |
Iron-sulfur | |
end case | |
case <FTGroup:1> or <FTGroup:2> or <FTGroup:4> or <FTGroup:5> | |
4Fe-4S | |
end case |
Gene Ontology
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case <FTGroup:1> or <FTGroup:2> or <FTGroup:3> or <FTGroup:4> or <FTGroup:5> | |
GO:0005506; Molecular function:iron ion binding | |
end case | |
case <FTGroup:3> | |
GO:0016151; Molecular function:nickel cation binding | |
end case | |
GO:0018492; Molecular function:carbon-monoxide dehydrogenase (acceptor) activity | |
case <OCellular component:Methanosarcinaceae> | |
GO:0019385; Biological process:methanogenesis, from acetate | |
end case |
Cross-references
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Pfam | PF00037; Fer4; 2; |
Pfam | PF03063; Prismane; 1; |
PRINTS | PR00353; 4FE4SFRDOXIN; 1; |
NCBIfam | TIGR00314; CdhA; 1; |
PROSITE | PS00198; 4FE4S_FER_1; 2; |
PROSITE | PS51379; 4FE4S_FER_2; 2; |
Features
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From: ACDA1_METBF (Q46G04) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 73 | 73 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="1" /ligand_note="ligand shared between dimeric partners" |
C | 1 | |||||||
BINDING | 76 | 76 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="2" |
C | 2 | |||||||
BINDING | 77 | 77 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="1" /ligand_note="ligand shared between dimeric partners" |
C | 1 | |||||||
BINDING | 79 | 79 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="2" |
C | 2 | |||||||
BINDING | 84 | 84 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="2" |
C | 2 | |||||||
BINDING | 94 | 94 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="2" |
C | 2 | |||||||
BINDING | 250 | 250 | /ligand="[Ni-4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:47739" |
H | 3 | |||||||
BINDING | 278 | 278 | /ligand="[Ni-4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:47739" |
C | 3 | |||||||
BINDING | 323 | 323 | /ligand="[Ni-4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:47739" |
C | 3 | |||||||
BINDING | 417 | 417 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="3" |
C | 4 | |||||||
BINDING | 420 | 420 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="3" |
C | 4 | |||||||
BINDING | 423 | 423 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="3" |
C | 4 | |||||||
BINDING | 427 | 427 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="4" |
C | 5 | |||||||
BINDING | 455 | 455 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="4" |
C | 5 | |||||||
BINDING | 458 | 458 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="4" |
C | 5 | |||||||
BINDING | 461 | 461 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="4" |
C | 5 | |||||||
BINDING | 465 | 465 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="3" |
C | 4 | |||||||
BINDING | 523 | 523 | /ligand="[Ni-4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:47739" |
C | 3 | |||||||
BINDING | 552 | 552 | /ligand="[Ni-4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:47739" |
C | 3 | |||||||
BINDING | 587 | 587 | /ligand="[Ni-4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:47739" |
C | 3 | |||||||
BINDING | 117 | 117 | /ligand="CO" /ligand_id="ChEBI:CHEBI:17245" |
H |
Additional information
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Size range | 632-807 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |