| Accession | TIGR01583 |
| Name | formate-DH-gamm |
| Function | formate dehydrogenase, gamma subunit |
| Trusted Cutoff | 115.85 |
| Domain Trusted Cutoff | 115.85 |
| Noise Cutoff | 56.10 |
| Domain Noise Cutoff | 56.10 |
| Isology Type | equivalog |
| EC Number | 1.2.1.2 |
| HMM Length | 204 |
| Mainrole Category | Energy metabolism |
| Subrole Category | Anaerobic |
| Gene Ontology Term | GO:0008863: formate dehydrogenase (NAD+) activity molecular_function |
| | GO:0009055: electron carrier activity molecular_function |
| | GO:0009061: anaerobic respiration biological_process |
| | GO:0009326: formate dehydrogenase complex cellular_component |
| Author | Selengut J |
| Entry Date | Jul 10 2002 11:59AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model represents the gamma chain of the gamma proteobacteria (and Aquifex aolicus) formate dehydrogenase. This subunit is integral to the cytoplasmic membrane, consisting of 4 transmembrane helices, and receives electrons from the beta subunit. The entire E. coli formate dehydrogenase N (nitrate-inducible form) has been crystallized [1]. The gamma subunit contains two cytochromes, heme b(P) and heme b(C) near the periplasmic and cytoplasmic sides of the membrane respectively. The electron acceptor quinone binds at the cytoplasmic heme histidine ligand.
NiFe-hydrogenase and thiosulfate reductase contain homologous gamma subunits, and these can be found scoring in the noise of this model. |
| References | RN [1]
RM PMID: 11884747
RT Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
RA Jormakka M, Tornroth S, Byrne B, Iwata S.
RL Science. 2002 Mar 8;295(5561):1863-8. |
