CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.10 | Arc Repressor Mutant, subunit A |
|
1.10.10.920 |
Domain Context
CATH Clusters
| Superfamily | 1.10.10.920 |
| Functional Family | Coproporphyrinogen-III oxidase |
Enzyme Information
| 1.3.98.3 |
Coproporphyrinogen dehydrogenase.
based on mapping to UniProt P32131
Coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO(2) + 2 L-methionine + 2 5'-deoxyadenosine.
-!- Differs from EC 1.3.3.3 by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant. -!- Occurs mainly in bacteria, whereas eukaryotes use the oxygen- dependent oxidase. -!- The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl; this radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. -!- This conversion, -.CH-CH(2)-COO- -> -CH=CH(2) + CO(2) + e(-) replaces the electron initially used. -!- Formerly EC 1.3.99.22.
|
UniProtKB Entries (1)
| P32131 |
HEMN_ECOLI
Escherichia coli K-12
Oxygen-independent coproporphyrinogen III oxidase
|
PDB Structure
| PDB | 1OLT |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of Coproporphyrinogen III Oxidase Reveals Cofactor Geometry of Radical Sam Enzymes
Embo J.
|
