| Accession | TIGR01350 |
| Name | lipoamide_DH |
| Function | dihydrolipoyl dehydrogenase |
| Gene Symbol | lpdA |
| Trusted Cutoff | 408.80 |
| Domain Trusted Cutoff | 408.80 |
| Noise Cutoff | 400.75 |
| Domain Noise Cutoff | 400.75 |
| Isology Type | equivalog |
| EC Number | 1.8.1.4 |
| HMM Length | 461 |
| Gene Ontology Term | GO:0004148: dihydrolipoyl dehydrogenase activity molecular_function |
| | GO:0005624: membrane fraction cellular_component |
| | GO:0006096: glycolysis biological_process |
| | GO:0045454: cell redox homeostasis biological_process |
| | GO:0051068: dihydrolipoamide metabolic process biological_process |
| Author | Haft DH |
| Entry Date | Sep 25 2001 10:59AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well.
The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide. |
| References | DR EXPERIMENTAL; SP|Q04829; Halobacterium volcanii
DR EXPERIMENTAL; SP|P00391; Escherichia coli
DR EXPERIMENTAL; SP:P11959; Bacillus stearothermophilus
DR EXPERIMENTAL; SP|P31023; Pisum sativum
DR EXCEPTION; GP:546360; ferric leghemoglobin reductase; Glycine max
DR EXCEPTION; GP:5823556; ferric leghemoglobin reductase; Vigna unguiculata |
| Genome Property | GenProp0178: glycine cleavage system (HMM) |
| | GenProp0630: 2-oxoglutarate dehydrogenase system (HMM) |
