Q9F8A8 · COOS2_CARHZ
- ProteinCarbon monoxide dehydrogenase 2
- GenecooS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids636 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).
Catalytic activity
- CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H+ + 2 reduced [2Fe-2S]-[ferredoxin]
Cofactor
Protein has several cofactor binding sites:
Note: Binds 3 [4Fe-4S] clusters per homodimer.
Note: Binds 2 [Ni-4Fe-5S] clusters per homodimer.
Activity regulation
Inactivated by O2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 47 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 48 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 51 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 56 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 70 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 261 | [Ni-4Fe-5S] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 295 | [Ni-4Fe-5S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 333 | [Ni-4Fe-5S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 446 | [Ni-4Fe-5S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 476 | [Ni-4Fe-5S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 526 | [Ni-4Fe-5S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | carbon-monoxide dehydrogenase (acceptor) activity | |
Molecular Function | carbon-monoxide dehydrogenase (ferredoxin) activity | |
Molecular Function | hydroxylamine reductase activity | |
Molecular Function | nickel cation binding | |
Molecular Function | peroxidase 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 2
- EC number
- Short namesCODH 2
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Thermoanaerobacterales > Thermoanaerobacteraceae > Carboxydothermus
Accessions
- Primary accessionQ9F8A8
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Loosely attached to the membrane, probably via CooF.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000157138 | 2-636 | Carbon monoxide dehydrogenase 2 | |||
Sequence: AKQNLKSTDRAVQQMLDKAKREGIQTVWDRYEAMKPQCGFGETGLCCRHCLQGPCRINPFGDEPKVGICGATAEVIVARGLDRSIAAGAAGHSGHAKHLAHTLKKAVQGKAASYMIKDRTKLHSIAKRLGIPTEGQKDEDIALEVAKAALADFHEKDTPVLWVTTVLPPSRVKVLSAHGLIPAGIDHEIAEIMHRTSMGCDADAQNLLLGGLRCSLADLAGCYMGTDLADILFGTPAPVVTESNLGVLKADAVNVAVHGHNPVLSDIIVSVSKEMENEARAAGATGINVVGICCTGNEVLMRHGIPACTHSVSQEMAMITGALDAMILDYQCIQPSVATIAECTGTTVITTMEMSKITGATHVNFAEEAAVENAKQILRLAIDTFKRRKGKPVEIPNIKTKVVAGFSTEAIINALSKLNANDPLKPLIDNVVNGNIRGVCLFAGCNNVKVPQDQNFTTIARKLLKQNVLVVATGCGAGALMRHGFMDPANVDELCGDGLKAVLTAIGEANGLGGPLPPVLHMGSCVDNSRAVALVAALANRLGVDLDRLPVVASAAEAMHEKAVAIGTWAVTIGLPTHIGVLPPITGSLPVTQILTSSVKDITGGYFIVELDPETAADKLLAAINERRAGLGLPW |
Interaction
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
- Length636
- Mass (Da)66,914
- Last updated2007-01-23 v4
- Checksum61C1011E86022A63
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 528 | in Ref. 1; AAG29809 | ||||
Sequence: D → H | ||||||
Sequence conflict | 532 | in Ref. 1; AAG29809 | ||||
Sequence: A → S | ||||||
Sequence conflict | 544 | in Ref. 1; AAG29809 | ||||
Sequence: G → W | ||||||
Sequence conflict | 547 | in Ref. 1; AAG29809 | ||||
Sequence: L → M | ||||||
Sequence conflict | 558 | in Ref. 1; AAG29809 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 583 | in Ref. 1; AAG29809 | ||||
Sequence: L → F | ||||||
Sequence conflict | 615-617 | in Ref. 1; AAG29809 | ||||
Sequence: ETA → VQQR | ||||||
Sequence conflict | 636 | in Ref. 1; AAG29809 | ||||
Sequence: W → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF249899 EMBL· GenBank· DDBJ | AAG29809.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP000141 EMBL· GenBank· DDBJ | ABB15588.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF244619 EMBL· GenBank· DDBJ | AAG23568.1 EMBL· GenBank· DDBJ | Genomic DNA |