{PDOC00335}
{PS01216; SUCCINYL_COA_LIG_1}
{PS00399; SUCCINYL_COA_LIG_2}
{PS01217; SUCCINYL_COA_LIG_3}
{BEGIN}
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* ATP-citrate lyase / succinyl-CoA ligases signatures *
*******************************************************

Four different enzymes  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 (EC 2.3.3.8) [1], 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)  (EC 6.2.1.4)  [2]  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) (EC 6.2.1.5) [3]  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.
 - Malate-CoA   ligase (EC 6.2.1.9) (malyl-CoA synthetase) [4], 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.

We developed three signature patterns for these enzymes, the first 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.
The second pattern, which is located some 50 residues to the C-terminal of the
first one, includes the active site phosphorylated histidine residue. The last
pattern corresponds  to  a  conserved  region located in the first half of ATP
citrate lyase  and in the beta subunits of succinyl-CoA ligases and malate-CoA
ligase.

-Consensus pattern: S-[KR]-S-G-[GT]-[LIVM]-[GST]-x-[EQ]-x(8,10)-G-x(4)-[LIVM]-
                    [GA]-[LIVM]-G-G-D
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: G-x(2)-A-x(4,7)-[RQT]-[LIVMF]-G-H-[AS]-[GH]
                    [H is the phosphorylated active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: G-x-[IVT]-x(2)-[LIVMF]-x-[NAK]-[GS]-[GA]-G-[LMAI]-[STAV]-
                    x(4)-[DN]-x-[LIVM]-x(3,4)-[GD]-[GREAK]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2006 / Pattern revised.

[ 1] Elshourbagy N.A., Near J.C., Kmetz P.J., Wells T.N., Groot P.H.,
     Saxty B.A., Hughes S.A., Franklin M., Gloger I.S.
     "Cloning and expression of a human ATP-citrate lyase cDNA."
     Eur. J. Biochem. 204:491-499(1992).
     PubMed=1371749
[ 2] Bailey D.L., Wolodko W.T., Bridger W.A.
     "Cloning, characterization, and expression of the beta subunit of pig
     heart succinyl-CoA synthetase."
     Protein Sci. 2:1255-1262(1993).
     PubMed=8401211
[ 3] Buck D., Spencer M.E., Guest J.R.
     "Primary structure of the succinyl-CoA synthetase of Escherichia
     coli."
     Biochemistry 24:6245-6252(1985).
     PubMed=3002435
[ 4] Chistoserdova L.V., Lidstrom M.E.
     "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."
     J. Bacteriol. 176:7398-7404(1994).
     PubMed=7961516

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