CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.15 | ATP Synthase; domain 1 |
|
2.60.15.10 | F0F1 ATP synthase delta/epsilon subunit, N-terminal |
Domain Context
CATH Clusters
| Superfamily | F0F1 ATP synthase delta/epsilon subunit, N-terminal |
| Functional Family | ATP synthase epsilon chain |
Enzyme Information
| 3.6.3.14 |
H(+)-transporting two-sector ATPase.
based on mapping to UniProt P0A6E6
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
-!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34.
|
UniProtKB Entries (1)
| P0A6E6 |
ATPE_ECOLI
Escherichia coli K-12
ATP synthase epsilon chain
|
PDB Structure
| PDB | 1AQT |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli.
Structure
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