Accession | TIGR00175 |
Name | mito_nad_idh |
Function | isocitrate dehydrogenase, NAD-dependent |
Trusted Cutoff | 432.40 |
Domain Trusted Cutoff | 432.40 |
Noise Cutoff | 323.75 |
Domain Noise Cutoff | 323.75 |
Isology Type | equivalog |
EC Number | 1.1.1.41 |
HMM Length | 334 |
Mainrole Category | Energy metabolism |
Subrole Category | TCA cycle |
Gene Ontology Term | GO:0004449: isocitrate dehydrogenase (NAD+) activity molecular_function |
| GO:0005962: mitochondrial isocitrate dehydrogenase complex (NAD+) cellular_component |
| GO:0006102: isocitrate metabolic process biological_process |
| GO:0045243: cytosolic isocitrate dehydrogenase complex (NAD+) cellular_component |
Author | Haft DH |
Entry Date | Apr 20 1999 2:08PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the multimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; the latter carbon, now adjacent to a carbonyl group, readily decarboxylates.
Mitochondrial NAD-dependent isocitrate dehydrogenases (IDH) resemble prokaryotic NADP-dependent IDH and 3-isopropylmalate dehydrogenase (an NAD-dependent enzyme) more closely than they resemble eukaryotic NADP-dependent IDH.
The mitochondrial NAD-dependent isocitrate dehydrogenase is believed to be an alpha(2)-beta-gamma heterotetramer. All subunits are homologous and found by this model.
The NADP-dependent IDH of Thermus aquaticus thermophilus strain HB8 resembles these NAD-dependent IDH, except for the residues involved in cofactor specificity, much more closely than it resembles other prokaryotic NADP-dependent IDH, including that of Thermus aquaticus strain YT1. |
References | A2 hmmalign
SE TIGR
GA hmmls
AL clustalw
BD build_dir/0253 |
Genome Property | GenProp0033: TCA cycle (HMM) |