CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.230 | Cytochrome p450-Terp; domain 2 |
|
1.10.230.10 | Cytochrome P450-Terp, domain 2 |
Domain Context
CATH Clusters
| Superfamily | Cytochrome P450-Terp, domain 2 |
| Functional Family | Citrate synthase |
Enzyme Information
| 2.3.3.16 |
Citrate synthase (unknown stereospecificity).
based on mapping to UniProt O34002
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA.
-!- This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C(2) of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3).
|
| 2.3.3.5 |
2-methylcitrate synthase.
based on mapping to UniProt O34002
Propanoyl-CoA + H(2)O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3- tricarboxylate + CoA.
-!- The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. -!- The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme is distinct from EC 2.3.3.1. -!- Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate. -!- Formerly EC 4.1.3.31.
|
UniProtKB Entries (1)
| O34002 |
PRPC_ABDS2
Antarctic bacterium DS2-3R
2-methylcitrate synthase
|
PDB Structure
| PDB | 1A59 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium.
Structure
|
