BAIT

ACC1

ABP2, FAS3, MTR7, acetyl-CoA carboxylase ACC1, L000000017, L000000014, L000000603, YNR016C
Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication
GO Process (3)
GO Function (2)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

ACC1

ABP2, FAS3, MTR7, acetyl-CoA carboxylase ACC1, L000000017, L000000014, L000000603, YNR016C
Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication
GO Process (3)
GO Function (2)
GO Component (2)
Saccharomyces cerevisiae (S288c)

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.

Zhang H, Yang Z, Shen Y, Tong L

Acetyl-coenzyme A carboxylases (ACCs) are required for the biosynthesis and oxidation of long-chain fatty acids. They are targets for therapeutics against obesity and diabetes, and several herbicides function by inhibiting their carboxyltransferase (CT) domain. We determined the crystal structure of the free enzyme and the coenzyme A complex of yeast CT at 2.7 angstrom resolution and found that it comprises ... [more]

Science Mar. 28, 2003; 299(5615);2064-7 [Pubmed: 12663926]

Throughput

  • Low Throughput

Curated By

  • BioGRID