| IED ID | IndEnz0018001007 |
| Enzyme Type ID | peroxidase001007 |
| Protein Name |
Carbon monoxide dehydrogenase 1 CODH 1 EC 1.2.7.4 |
| Gene Name | cooS1 MA_3282 |
| Organism | Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Methanomicrobia Methanosarcinales Methanosarcinaceae Methanosarcina Methanosarcina acetivorans Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) |
| Enzyme Sequence | MGKEMKQTAFEKSIDSASQIMLQKAEDEGIETAWDRYEQQLPQCSFGQLGICCRNCNMGPCRIDPFGEGTEKGICGATADIIVARNLLRMIAAGAAAHSDHARDAVLTFKKMSEGKAGSYRIKDEAKLYSLASEYGISAEEKSREEVAVELASALLSEFGKQEGPILCTKRAPESRLKLWSELGIEPRGIDREIVECMHRTHIGVDNDATHILLHGLRTSLSDGWGGSMIATEIQDVLFGTPEPKKSTVNLGVLSHDKVNVIVHGHEPILSEMIVEAAEDPELLELAEEKGATGINVAGICCTGNETLMRHGTPIAGTFLQQELAVITGAVEAMVVDVQCIMPSLGNLTGCYHTKFISTSPKADFPGTARMEFHEEEAYATAKEIVKAAVENFPNRNLKKVSIPEEKQECMVGFSAEAILKALGGSPAPLIEAIAGGAIKGIGAVVGCNNVKIQHNYGHVNLVKELIKNNVLVVTTGCNAIACAEAGLLVPEAAALAGDGLKGVCEALGIPPVLHMGSCVDISRILVLASAVANSLGVDISDLPAAGAAPEWMSEKAVSIGAYVVSSGVFTVLGTIPPVLGSQAVTALLTKGLDGVIGASFAVEPDPFKAADLMLEHIEGKRKALGLK |
| Enzyme Length | 628 |
| Uniprot Accession Number | Q8TKW2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4; Evidence={ECO:0000250|UniProtKB:Q9F8A8}; |
| DNA Binding | |
| EC Number | 1.2.7.4 |
| Enzyme Function | FUNCTION: CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH). {ECO:0000250|UniProtKB:Q9F8A8}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (12) |
| Keywords | 4Fe-4S;Iron;Iron-sulfur;Metal-binding;Nickel;Oxidoreductase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 66,367 |
| Kinetics | |
| Metal Binding | METAL 44; /note=Iron-sulfur (4Fe-4S) 1; shared with dimeric partner; /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 52; /note=Iron-sulfur (4Fe-4S) 1; shared with dimeric partner; /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 53; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 56; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 61; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 75; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 266; /note=Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 302; /note=Nickel-iron-sulfur (Ni-4Fe-5S); /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 340; /note=Nickel-iron-sulfur (Ni-4Fe-5S); /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 448; /note=Nickel-iron-sulfur (Ni-4Fe-5S); /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 478; /note=Nickel-iron-sulfur (Ni-4Fe-5S); /evidence=ECO:0000250|UniProtKB:Q9F8A8; METAL 519; /note=Nickel-iron-sulfur (Ni-4Fe-5S); /evidence=ECO:0000250|UniProtKB:Q9F8A8 |
| Rhea ID | RHEA:21040 |
| Cross Reference Brenda |