| IED ID | IndEnz0018000128 |
| Enzyme Type ID | peroxidase000128 |
| Protein Name |
Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 ACDS complex subunit alpha 1 EC 1.2.7.4 ACDS complex carbon monoxide dehydrogenase subunit alpha 1 ACDS CODH subunit alpha 1 |
| Gene Name | cdhA1 MA_1016 |
| 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 | MSKLTTGSFSIEDLESVQITINNIVGAAKEAAEEKAKELEKAGPTLFPGLESYRDDWNFKLLDRYEPVITPMCDQCCYCTYGPCDLSGNKRGACGIDMLGHNGREFFLRVITGTACHAAHGRHLLDHLIETFGEDLPLNLGQSNVLTPNITISTGLSPKNLGEIKPAMEFVEEQLTQLLATVHAGQESAEIDYDSKALFSGSLDHVGMEISDVVQVAAYDFPKADPEAPLIEIGMGTIDKSKPFLCVIGHNVGGVTYMMDYMEEHDLTDKMEIAGLCCTAIDLSRYKEADRRPPYAKVIGSMSKELKVIRSGMPDVIVVDEQCVRGDIVPEAQKLKIPVIASNAKIMYGLPNRTDANVDDVVEELKSGAIPGCVMLDYDKLGELCIRLTMEMGPIRDAEGITAIPTDEEFADWVAKCADCGACMIACPEELDIPEAMGFAKEGDFSYLEELHDQCIGCRRCEQVCKKEIPILNIIEKVAQKQIAEEKGWMRAGRGQVSDAEIRAEGLNLVMGTTPGIIAIIGCPNYAEGTKDVYYIAEEFLKRNFIVVTTGCGAMDIGMFKDEDGKTLYERFPGGFECGGLVNIGSCVSNAHITGAAEKVAAIFAQRTLEGNLAEISDYILNRVGACGLAWGAFSQKASSIGTGCNILGIPAVLGPHSSKYRRALIAKTYEEDKWKVYDARNGQEMPIPPAPEFLLTTAETWQEAIPMMAKACIRPSDNSMGRSIKLTHWMELHKKYLGKDPEDWWKFVRNEADLPLAKREALLKELESKHGWEIDWKKKKIISGPKIKFDVSAQPTNLKRLCKEA |
| Enzyme Length | 806 |
| Uniprot Accession Number | Q8TRZ4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 117; /note=Carbon monoxide; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01137 |
| 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:0000255|HAMAP-Rule:MF_01137}; |
| DNA Binding | |
| EC Number | 1.2.7.4 |
| Enzyme Function | FUNCTION: Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. {ECO:0000255|HAMAP-Rule:MF_01137}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: One-carbon metabolism; methanogenesis from acetate. {ECO:0000255|HAMAP-Rule:MF_01137}. |
| nucleotide Binding | |
| Features | Binding site (1); Chain (1); Domain (2); Metal binding (20) |
| Keywords | 4Fe-4S;Iron;Iron-sulfur;Metal-binding;Methanogenesis;Nickel;Oxidoreductase;Reference proteome;Repeat |
| 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 | 88,694 |
| Kinetics | |
| Metal Binding | METAL 73; /note=Iron-sulfur (4Fe-4S) 1; shared with dimeric partner; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 76; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 77; /note=Iron-sulfur (4Fe-4S) 1; shared with dimeric partner; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 79; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 84; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 94; /note=Iron-sulfur (4Fe-4S) 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 250; /note=Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 278; /note=Nickel-iron-sulfur (Ni-4Fe-4S); /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 323; /note=Nickel-iron-sulfur (Ni-4Fe-4S); /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 417; /note=Iron-sulfur (4Fe-4S) 3; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 420; /note=Iron-sulfur (4Fe-4S) 3; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 423; /note=Iron-sulfur (4Fe-4S) 3; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 427; /note=Iron-sulfur (4Fe-4S) 4; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 455; /note=Iron-sulfur (4Fe-4S) 4; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 458; /note=Iron-sulfur (4Fe-4S) 4; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 461; /note=Iron-sulfur (4Fe-4S) 4; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 465; /note=Iron-sulfur (4Fe-4S) 3; /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 523; /note=Nickel-iron-sulfur (Ni-4Fe-4S); /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 552; /note=Nickel-iron-sulfur (Ni-4Fe-4S); /evidence=ECO:0000255|HAMAP-Rule:MF_01137; METAL 587; /note=Nickel-iron-sulfur (Ni-4Fe-4S); /evidence=ECO:0000255|HAMAP-Rule:MF_01137 |
| Rhea ID | RHEA:21040 |
| Cross Reference Brenda |