8C0Z
CryoEM structure of a tungsten-containing aldehyde oxidoreductase from Aromatoleum aromaticum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| A | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
| A | 0043795 | molecular_function | glyceraldehyde oxidoreductase activity |
| A | 0047770 | molecular_function | carboxylate reductase activity |
| A | 0047985 | molecular_function | hydrogen dehydrogenase activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0140087 | molecular_function | acetaldehyde dehydrogenase (NAD+) activity |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| B | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
| B | 0043795 | molecular_function | glyceraldehyde oxidoreductase activity |
| B | 0047770 | molecular_function | carboxylate reductase activity |
| B | 0047985 | molecular_function | hydrogen dehydrogenase activity |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0140087 | molecular_function | acetaldehyde dehydrogenase (NAD+) activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CvGCKvCTiACP |
| Chain | Residue | Details |
| C | CYS86-PRO97 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 57 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"37267359","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8C0Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 58 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 62 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 58 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 50 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
