Description

IPR033847 is a ATP-citrate lyase/succinyl-CoA ligase, conserved site.

<p>There are four different enzymes that share a similar catalytic mechanism which involves the phosphorylation by ATP (or GTP) of a specific histidine residue in the active site. These enzymes are:</p> <ul><li>ATP citrate-lyase ([ec:4.1.3.8]) [[cite:PUB00001411]], the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues, catalyses the formation of acetyl-CoA and oxaloacetate from citrate and CoA with the concomitant hydrolysis of ATP to ADP and phosphate. ATP-citrate lyase is a tetramer of identical subunits.</li> <li>Succinyl-CoA ligase (GDP-forming) ([ec:6.2.1.4]) [[cite:PUB00005004]] is a mitochondrial enzyme that catalyses the substrate level phosphorylation step of the tricarboxylic acid cycle: the formation of succinyl-CoA from succinate with a concomitant hydrolysis of GTP to GDP and phosphate. This enzyme is a dimer composed of an alpha and a beta subunits.</li> <li>Succinyl-CoA ligase (ADP-forming) ([ec:6.2.1.5]) [[cite:PUB00000280]] is a bacterial enzyme that during aerobic metabolism functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP. It can also function in the other direction for anabolic purposes. This enzyme is a tetramer composed of two alpha and two beta subunits.</li> <li>Malate-CoA ligase ([ec:6.2.1.9]) (malyl-CoA synthetase) [[cite:PUB00002257]], is a bacterial enzyme that forms malyl-CoA from malate and CoA with the concomitant hydrolysis of ATP to ADP and phosphate. Malate-CoA ligase is composed of two different subunits.</li></ul> <p>This entry corresponds to a glycine-rich conserved region, located in the second half of ATP citrate lyase and in the alpha subunits of succinyl-CoA ligases and malate-CoA ligase.</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 15

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: