CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.499 | Aconitase; domain 3 |
|
3.30.499.10 | Aconitase, domain 3 |
Domain Context
CATH Clusters
| Superfamily | Aconitase, domain 3 |
| Functional Family |
Enzyme Information
| 4.2.1.114 |
Methanogen homoaconitase.
based on mapping to UniProt Q58409
(R)-2-hydroxybutane-1,2,4-tricarboxylate = (1R,2S)-1-hydroxybutane-1,2,4- tricarboxylate.
-!- Catalyzes several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea. -!- In contrast to EC 4.2.1.36, this enzyme can catalyze both the dehydration of (R)-homocitrate to form cis-homoaconitate and the subsequent hydration reaction that forms homoisocitrate. -!- In addition to cis-homoaconitate, the enzyme can also catalyze the hydration of the physiological substrates dihomocitrate and trihomocitrate as well as the non-physiological substrate tetrahomocitrate. -!- Cis-aconitate and threo-DL-isocitrate cannot act as substrates, and (S)-homocitrate and trans-homoaconitate act as inhibitors of the enzyme.
|
UniProtKB Entries (1)
| Q58409 |
HACA_METJA
Methanocaldococcus jannaschii DSM 2661
Methanogen homoaconitase large subunit
|
PDB Structure
| PDB | 4KP2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii
Acta Crystallogr.,Sect.D
|
