CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.20 | Up-down Bundle | |
1.20.20 | F1FO ATP Synthase | |
1.20.20.10 | F1F0 ATP synthase subunit C |
Domain Context
CATH Clusters
Superfamily | F1F0 ATP synthase subunit C |
Functional Family | ATP synthase subunit c |
Enzyme Information
3.6.3.14 |
H(+)-transporting two-sector ATPase.
based on mapping to UniProt P68699
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.
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UniProtKB Entries (1)
P68699 |
ATPL_ECOLI
Escherichia coli K-12
ATP synthase subunit c
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PDB Structure
PDB | 1A91 |
External Links | |
Method | SOLUTION NMR |
Organism | Escherichia |
Primary Citation |
Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase.
Biochemistry
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