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RHORU:MDH
Contents
| Species (Taxon ID) | Rhodospirillum rubrum. (1085) | |
| Gene Name(s) | mdh | |
| Protein Name(s) | Malate dehydrogenase | |
| External Links | ||
| UniProt | P80459 | |
| GO | GO:0030060 GO:0004471 GO:0006099 | |
| Gene3D | 3.40.50.720 | |
| InterPro | IPR016040 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004471 |
malate dehydrogenase (decarboxylating) activity |
ECO:0000314 |
F |
Malate dehydrogenase is the citric acid cycle enzyme that catalyses the oxidation of malate to oxaloacetate. Figure 1 shows the enzyme activity for various time periods at 65 C. |
complete | |||||
| GO:0004471 |
malate dehydrogenase (decarboxylating) activity |
ECO:0000314 |
F |
Table 1 |
complete | |||||
|
enables |
GO:0004471 |
malate dehydrogenase (decarboxylating) (NAD+) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004471 |
malate dehydrogenase (decarboxylating) (NAD+) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0030060 |
L-malate dehydrogenase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Tayeh, MA & Madigan, MT (1988) Malate dehydrogenases in phototrophic purple bacteria. Thermal stability, amino acid composition and immunological properties. Biochem. J. 252 595-600 PubMed GONUTS page
- ↑ 2.0 2.1 Tayeh, MA & Madigan, MT (1987) Malate dehydrogenase in phototrophic purple bacteria: purification, molecular weight, and quaternary structure. J. Bacteriol. 169 4196-202 PubMed GONUTS page
b
