Home | Contact

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 β- 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].

November 1997 / First entry.

PROSITE methods (with tools and information) covered by this documentation:

COA_TRANSF_1, PS01273; Coenzyme A transferases signature 1  (PATTERN)

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.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01273 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01273 • Scan Swiss-Prot/TrEMBL entries against PS01273 • view ligand binding statistics

Matching PDB structures: 1K6D 1M3E 1O9L 1OOY ... [ALL]

COA_TRANSF_2, PS01274; Coenzyme A transferases signature 2  (PATTERN)

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.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01274 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01274 • Scan Swiss-Prot/TrEMBL entries against PS01274 • view ligand binding statistics

Matching PDB structures: 1M3E 1O9L 1OOY 1OOZ ... [ALL]

1	Authors	Parales R.E., Harwood C.S.
	Title	Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida.
	Source	J. Bacteriol. 174:4657-4666(1992).
	PubMed ID	1624453

2	Authors	Corthesy-Theulaz I.E., Bergonzelli G.E., Henry H., Bachmann D., Schorderet D.F., Blum A.L., Ornston L.N.
	Source	J. Biol. Chem. 272:25659-25667(1997).

3	Authors	Rochet J.C., Bridger W.A.
	Title	Identification of glutamate 344 as the catalytic residue in the active site of pig heart CoA transferase.
	Source	Protein Sci. 3:975-981(1994).
	PubMed ID	7915164

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to

Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)

SIB Swiss Institute of Bioinformatics | Disclaimer