P27989 · DCMB_MOOTH
- ProteinCarbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids674 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
The beta subunit (this protein) generates CO from CO2, while the alpha subunit combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the alpha subunit by a corrinoid iron-sulfur protein.
Catalytic activity
- CO + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O = 2 reduced [2Fe-2S]-[ferredoxin] + CO2 + 2 H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [Ni-Fe-S] cluster per subunit.
Note: Binds 2 [4Fe-4S] clusters per homodimer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 59 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 67 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 68 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 71 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 76 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 90 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 283 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 317 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 355 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 470 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 500 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 550 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | anaerobic carbon-monoxide dehydrogenase activity | |
Molecular Function | hydroxylamine reductase activity | |
Molecular Function | nickel cation binding | |
Molecular Function | peroxidase activity | |
Biological Process | carbon fixation | |
Biological Process | generation of precursor metabolites and energy | |
Biological Process | response to hydrogen peroxide |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta
- EC number
- Short namesCODH subunit; CODH/ACS; Carbon monoxide dehydrogenase subunit
Organism names
- Taxonomic lineageBacteria > Bacillota > Clostridia > Moorellales > Moorellaceae > Moorella
Accessions
- Primary accessionP27989
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000079808 | 1-674 | Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta | |||
Sequence: MPRFRDLSHNCRPSEAPRVMEPKNRDRTVDPAVLEMLVKSKDDKVITAFDRFVAQQPQCKIGYEGICCRFCMAGPCRIKATDGPGSRGICGASAWTIVARNVGLMILTGAAAHCEHGNHIAHALVEMAEGKAPDYSVKDEAKLKEVCRRVGIEVEGKSVLELAQEVGEKALEDFRRLKGEGEATWLMTTINEGRKEKFRTHNVVPFGIHASISELVNQAHMGMDNDPVNLVFSAIRVALADYTGEHIATDFSDILFGTPQPVVSEANMGVLDPDQVNFVLHGHNPLLSEIIVQAAREMEGEAKAAGAKGINLVGICCTGNEVLMRQGIPLVTSFASQELAICTGAIDAMCVDVQCIMPSISAVAECYHTRIITTADNAKIPGAYHIDYQTATAIESAKTAIRMAIEAFKERKESNRPVYIPQIKNRVVAGWSLEALTKLLATQNAQNPIRVLNQAILDGELAGVALICGCNNLKGFQDNSHLTVMKELLKNNVFVVATGCSAQAAGKLGLLDPANVETYCGDGLKGFLKRLGEGANIEIGLPPVFHMGSCVDNSRAVDLLMAMANDLGVDTPKVPFVASAPEAMSGKAAAIGTWWVSLGVPTHVGTMPPVEGSDLIYSILTQIASDVYGGYFIFEMDPQVAARKILDALEYRTWKLGVHKEVAERYETKLCQGY |
Interaction
Subunit
Tetramer of two alpha and two beta chains.
Structure
Sequence
- Sequence statusComplete
- Length674
- Mass (Da)72,924
- Last updated1992-08-01 v1
- Checksum54BA3D816C25F9FC
Keywords
- Technical term