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Database: PROSITE(DOC)
Entry: PDOC00980
LinkDB: PDOC00980
Original site: PDOC00980 
{PDOC00980}
{PS01273; COA_TRANSF_1}
{PS01274; COA_TRANSF_2}
{BEGIN}
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* Coenzyme A transferases signatures *
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Coenzyme A  (CoA)  transferases are enzymes catalyzing the reversible transfer
of CoA from one carboxylic acid to another.  They have been identified in many
prokaryotes and in mammalian tissues. They belong to an evolutionary conserved
[1,2] family of proteins that consist of:

 - Succinyl  CoA:3-oxoacid  CoA  transferase  (EC  2.8.3.5)  (SCOT),  which is
   responsible for  the  formation  of  acetoacetyl  CoA  by transfer of a CoA
   moiety from  succinyl-CoA  to a 3-oxoacid, usually acetoacetate.  In higher
   eukaryotes it  is  a  mitochondrial  enzyme  which  plays a crucial role in
   ketone body metabolism. It has also been found in bacteria.
 - Bacterial 3-oxoadipate CoA-transferase  (EC 2.8.3.6) which  carries out the
   penultimate  step in the  conversion of benzoate  and 4-hydroxybenzoate  to
   tricarboxylic acid  cycle  intermediates  in  bacteria  utilizing the beta-
   ketoadipate pathway.
 - Bacterial acetate CoA-transferase (EC 2.8.3.8).
 - Clostridial  butyrate-acetoacetate CoA-transferase (EC 2.8.3.9), which acts
   mainly to detoxify the medium by removing the acetate and butyrate excreted
   earlier in the fermentation.

The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd
each while  eukaryotic  SCOT  consist of a single chain which is colinear with
the two bacterial subunits.

We developed  two  signature patterns for these enzymes. The first corresponds
to a region in  the N-terminal of  the A subunit that may be implicated in the
binding of  CoA  to  the  enzyme. The second corresponds to a region in the N-
terminal of  the  B  subunit  and contains a glutamate that is involved in the
catalytic mechanism [3].

-Consensus pattern: [DN]-[GN]-x(2)-[LIVMFA](3)-G-G-F-x(3)-G-x-P
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [LF]-[HQ]-S-E-N-G-[LIVF](2)-[GA]
                    [E is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: November 1997 / First entry.

[ 1] Parales R.E., Harwood C.S.
     "Characterization of the genes encoding beta-ketoadipate:
     succinyl-coenzyme A transferase in Pseudomonas putida."
     J. Bacteriol. 174:4657-4666(1992).
     PubMed=1624453
[ 2] Corthesy-Theulaz I.E., Bergonzelli G.E., Henry H., Bachmann D.,
     Schorderet D.F., Blum A.L., Ornston L.N.
     J. Biol. Chem. 272:25659-25667(1997).
[ 3] Rochet J.C., Bridger W.A.
     "Identification of glutamate 344 as the catalytic residue in the
     active site of pig heart CoA transferase."
     Protein Sci. 3:975-981(1994).
     PubMed=7915164
{END}
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