P19913 · DCML_HYDPS
- ProteinCarbon monoxide dehydrogenase large chain
- GenecutL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids803 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the oxidation of carbon monoxide to carbon dioxide.
Catalytic activity
- a quinone + CO + H2O = a quinol + CO2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Cu+ ion per subunit.
Note: Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | carbon-monoxide dehydrogenase (acceptor) activity | |
Molecular Function | carbon-monoxide oxygenase activity | |
Molecular Function | copper ion binding | |
Molecular Function | iron ion binding | |
Molecular Function | molybdenum ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarbon monoxide dehydrogenase large chain
- EC number
- Short namesCO dehydrogenase subunit L; CO-DH L
Gene names
Organism names
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Hydrogenophaga
Accessions
- Primary accessionP19913
- Secondary accessions
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000079809 | 1-803 | Carbon monoxide dehydrogenase large chain | |||
Sequence: MNAPVQDAEARELALAGMRPRACAKEDARFIQGKGNYVDDIKMPGMLHMDIVRAPIAHGRIKKIHKDAALAMPGVHAVLTAEDLKPLKLHWMPTLAGDVAAVLADEKVHFQMQEVAIVIADDRYIAADAVEAVKVEYDELPVVIDPIDALKPDAPVLREDLAGKTSGAHGPREHHNHIFTWGAGDKAATDAVFANAPVTVSQHMYYPRVHPCPLETCGCVASFDPIKGDLTTYITSQAPHVVRTVVSMLSGIPESKVRIVSPDIGGGFGNKVGIYPGYVCAIVASIVLGRPVKWVEDRVENISTTAFARDYHMDGELAATPDGKILGLRVNVVADHGAFDACADPTKFPAGLFHICSGSYDIPRAHCSVKGVYTNKAPGGVAYRCSFRVTEAVYLIERMVDVLAQKLNMDKAEIRAKNFIRKEQFPYTTQFGFEYDSGDYHTALKKVLDAVDYPAWRAEQAARRADPNSPTLMGIGLVTFTEVVGAGPSKMCDILGVGMFDSCEIRIHPTGSAIARMGTITQGQGHQTTYAQIIATELGIPSEVIQVEEGDTSTAPYGLGTYGSRSTPVAGAAIALAARKIHAKARKIAAHMLEVNENDLDWEVDRFKVKGDDSKFKTMADIAWQAYHQPPAGLEPGLEAVHYYDPPNFTYPFGIYLCVVDIDRATGETKVRRFYALDDCGTRINPMIIEGQIHGGLTEGYAVAMGQQMPFDAQGNLLGNTLMDYFLPTAVETPHWETDHTVTPSPHHPIGAKGVAESPHVGSIPTFTAAVVDAFAHVGVTHLDMPHTSYRVWKSLKEHNLAL | ||||||
Modified residue | 384 | 4-hydroxyarginine | ||||
Sequence: R |
Keywords
- PTM
Interaction
Subunit
Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
Structure
Sequence
- Sequence statusComplete
- Length803
- Mass (Da)87,229
- Last updated2002-07-11 v2
- Checksum3CD5FE205DBE0712
Keywords
- Technical term