InterPro : IPR005810

Name  Succinyl-CoA ligase, alpha subunit Short Name  CoA_lig_alpha
Type  Family Description  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: ATP citrate-lyase () [], the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues, catalyzes 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; Succinyl-CoA ligase (GDP-forming) () []is a mitochondrial enzyme that catalyzes 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; Succinyl-CoA ligase (ADP-forming) () []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; and Malate-CoA ligase () (malyl-CoA synthetase) [], 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.This entry corresponds to two regions, a glycine-rich conserved region, located in the second half of ATP citratelyase and in the alpha subunits of succinyl-CoA ligases and malate-CoA ligase; and the active site phosphorylated histidine residue, which is located some 50 residues to the C-terminal of the first region.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

3 Contains

Id Name Short Name Type
IPR005811 ATP-citrate lyase/succinyl-CoA ligase CoA_ligase Domain
IPR003781 CoA-binding CoA-bd Domain
IPR017440 ATP-citrate lyase/succinyl-CoA ligase, active site Cit_synth/succinyl-CoA_lig_AS Active_site

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Buck D Primary structure of the succinyl-CoA synthetase of Escherichia coli. 1985 Biochemistry 24 6245-52
Elshourbagy NA Cloning and expression of a human ATP-citrate lyase cDNA. 1992 Eur J Biochem 204 491-9
Chistoserdova LV Genetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB. 1994 J Bacteriol 176 7398-404
Bailey DL Cloning, characterization, and expression of the beta subunit of pig heart succinyl-CoA synthetase. 1993 Protein Sci 2 1255-62



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)