P31896 · COOS_RHORU
- ProteinCarbon monoxide dehydrogenase
- GenecooS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids639 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).
Miscellaneous
Methyl viologen can act as acceptor. Inactivated by O2.
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 3 [4Fe-4S] clusters per homodimer.
Note: Binds 2 [Ni-4Fe-4S] clusters per homodimer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 41 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 49 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 50 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 53 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 58 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 72 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 265 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 300 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 338 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 451 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 481 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 531 | [Ni-4Fe-4S] cluster (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | anaerobic carbon-monoxide dehydrogenase activity | |
Molecular Function | ferrous iron binding | |
Molecular Function | hydroxylamine reductase activity | |
Molecular Function | nickel cation binding | |
Molecular Function | oxidoreductase activity | |
Molecular Function | peroxidase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | generation of precursor metabolites and energy | |
Biological Process | response to hydrogen peroxide |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarbon monoxide dehydrogenase
- EC number
- Short namesCODH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Rhodospirillum
Accessions
- Primary accessionP31896
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Note: Loosely attached to the inner membrane, probably via CooF.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 265 | Great decrease in activity; diminishes incorporation of nickel. Displays hydroxylamine reductase activity. | |||
Mutagenesis | 531 | Displays hydrogenase activity. | |||
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Chain | PRO_0000157139 | 2-639 | Carbon monoxide dehydrogenase | ||
Expression
Induction
By carbon monoxide; under anaerobic conditions.
Interaction
Subunit
Homodimer.
Structure
Family & Domains
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.
Sequence similarities
Belongs to the Ni-containing carbon monoxide dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length639
- Mass (Da)66,854
- Last updated1993-07-01 v1
- MD5 Checksum44798BA803382E8E78B661BE2362683E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U65510 EMBL· GenBank· DDBJ | AAC45123.1 EMBL· GenBank· DDBJ | Genomic DNA |