CATH Classification
Level | CATH Code | Description |
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2 | Mainly Beta |
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2.40 | Beta Barrel |
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2.40.10 | Thrombin, subunit H |
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2.40.10.170 |
Domain Context
CATH Clusters
Superfamily | 2.40.10.170 |
Functional Family |
Enzyme Information
7.1.2.2 |
H(+)-transporting two-sector ATPase.
based on mapping to UniProt Q2STE9
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2).
-!- 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 and EC 3.6.3.14.
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UniProtKB Entries (1)
Q2STE9 |
ATPB1_BURTA
Burkholderia thailandensis E264
ATP synthase subunit beta 1
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PDB Structure
PDB | 4Q4L |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal structure of an ATP synthase subunit beta 1 (F1-B1) from Burkholderia thailandensis
TO BE PUBLISHED
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