P31896 · COOS_RHORU

  • Protein
    Carbon monoxide dehydrogenase
  • Gene
    cooS
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Cofactor

Protein has several cofactor binding sites:
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 3 [4Fe-4S] clusters per homodimer.
[Ni-4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:47739 )

Note: Binds 2 [Ni-4Fe-4S] clusters per homodimer.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site41[4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site49[4Fe-4S] cluster 1 (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site50[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site53[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site58[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site72[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site265[Ni-4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site300[Ni-4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site338[Ni-4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site451[Ni-4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site481[Ni-4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site531[Ni-4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Molecular Function3 iron, 4 sulfur cluster binding
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionanaerobic carbon-monoxide dehydrogenase activity
Molecular Functionferrous iron binding
Molecular Functionhydroxylamine reductase activity
Molecular Functionnickel cation binding
Molecular Functionoxidoreductase activity
Molecular Functionperoxidase activity
Molecular Functionprotein homodimerization activity
Biological Processgeneration of precursor metabolites and energy
Biological Processresponse to hydrogen peroxide

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Carbon monoxide dehydrogenase
  • EC number
  • Short names
    CODH

Gene names

    • Name
      cooS

Organism names

  • Taxonomic identifier
  • Strain
    • UR1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Rhodospirillum

Accessions

  • Primary accession
    P31896

Subcellular Location

Cell inner membrane ; Peripheral membrane protein
Note: Loosely attached to the inner membrane, probably via CooF.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis265Great decrease in activity; diminishes incorporation of nickel. Displays hydroxylamine reductase activity.
Mutagenesis531Displays hydrogenase activity.

PTM/Processing

Features

Showing features for initiator methionine, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001571392-639Carbon monoxide dehydrogenase

Expression

Induction

By carbon monoxide; under anaerobic conditions.

Interaction

Subunit

Homodimer.

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    639
  • Mass (Da)
    66,854
  • Last updated
    1993-07-01 v1
  • MD5 Checksum
    44798BA803382E8E78B661BE2362683E
MTHHDCAHCSSDACATEMLNLAEANSIETAWHRYEKQQPQCGFGSAGLCCRICLKGPCRIDPFGEGPKYGVCGADRDTIVARHLVRMIAAGTAAHSEHGRHIALAMQHISQGELHDYSIRDEAKLYAIAKTLGVATEGRGLLAIVGDLAAITLGDFQNQDYDKPCAWLAASLTPRRVKRLGDLGLLPHNIDASVAQTMSRTHVGCDADPTNLILGGLRVAMADLDGSMLATELSDALFGTPQPVVSAANLGVMKRGAVNIAVNGHNPMLSDIICDVAADLRDEAIAAGAAEGINIIGICCTGHEVMMRHGVPLATNYLSQELPILTGALEAMVVDVQCIMPSLPRIAECFHTQIITTDKHNKISGATHVPFDEHKAVETAKTIIRMAIAAFGRRDPNRVAIPAFKQKSIVGFSAEAVVAALAKVNADDPLKPLVDNVVNGNIQGIVLFVGCNTTKVQQDSAYVDLAKSLAKRNVLVLATGCAAGAFAKAGLMTSEATTQYAGEGLKGVLSAIGTAAGLGGPLPLVMHMGSCVDNSRAVALATALANKLGVDLSDLPLVASAPECMSEKALAIGSWAVTIGLPTHVGSVPPVIGSQIVTKLVTETAKDLVGGYFIVDTDPKSAGDKLYAAIQERRAGLGL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U65510
EMBL· GenBank· DDBJ
AAC45123.1
EMBL· GenBank· DDBJ
Genomic DNA

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