|
|
||
|
|
|
|
|
UniProt functional annotation for Q46G04 | ||
|
|
|
|
|
|
||
| UniProt code: Q46G04. |
|
||
| Organism: | |
Methanosarcina barkeri (strain Fusaro / DSM 804). |
| Taxonomy: | |
Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina. |
|
||
|
||
| 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. {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:6425262}. |
|
||
| 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; Evidence={ECO:0000255|HAMAP-Rule:MF_01137}; |
| Cofactor: | |
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675}; Note=Binds 7 [4Fe-4S] clusters per heterotetramer. {ECO:0000255|HAMAP- Rule:MF_01137, ECO:0000269|PubMed:18621675}; |
| Cofactor: | |
Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739; Evidence={ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675}; Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer. {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675}; |
| Activity regulation: | |
Carbon monoxide dehydrogenase activity is inhibited by KCN and is rapidly inactivated by O(2). {ECO:0000269|PubMed:6425262}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=5 mM for CO (at 37 degrees Celsius) {ECO:0000269|PubMed:6425262}; Vmax=1300 umol/min/mg enzyme for CO dehydrogenase activity using methyl viologen as electron acceptor (at 37 degrees Celsius) {ECO:0000269|PubMed:6425262}; |
| Pathway: | |
One-carbon metabolism; methanogenesis from acetate. {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000305|PubMed:6425262}. |
| Subunit: | |
Heterotetramer of two alpha and two epsilon subunits (PubMed:6425262). 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) (By similarity). {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:6425262, ECO:0000305|PubMed:18621675}. |
| Induction: | |
Up-regulated during growth on acetate. {ECO:0000269|PubMed:6425262}. |
| 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. {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000305|PubMed:18621675}. |
| Similarity: | |
Belongs to the Ni-containing carbon monoxide dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01137}. |
Annotations taken from UniProtKB at the EBI.