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* Acyltransferases ChoActase / COT / CPT family signatures *
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A number of eukaryotic acetyltransferases  can  be,  on  the basis of sequence
similarities, grouped together into a family. These enzymes are:

 - Choline o-acetyltransferase  (EC 2.3.1.6)   (ChoAcTase), an   enzyme   that
   catalyzes the biosynthesis of the neurotransmitter acetylcholine [1].
 - Carnitine o-acetyltransferase (EC 2.3.1.7) [2].
 - Peroxisomal carnitine octanoyltransferase (EC 2.3.1.-)  (COT), a fatty acid
   beta-oxidation pathway enzyme which is involved in the transport of medium-
   chain acyl-coenzyme A's from peroxisome to mitochondria [3].
 - Mitochondrial carnitine palmitoyltransferases I and II (EC 2.3.1.21) (CPT),
   enzymes involved in fatty acid metabolism and transport [4].

These three enzymes share many regions of sequence similarities.  As signature
patterns we  selected  two of these regions.  The  first one,  located  in the
N-terminal section of  these enzymes is characterized by the presence of three
[LIVM]-P dipeptides. The second region, located in the central  part  of these
enzymes is  characterized  by the conservation of a number of charged residues
including an  histidine  which  probably plays a crucial role in the catalytic
mechanism [5].

-Consensus pattern: L-P-x-[LIVMP]-P-[LIVM]-P-x-[LIVM]-x-[DENQAS]-[ST]-[LIVM]-
                    x(2)-Y
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.

-Consensus pattern: R-[FYW]-x-D-[KA]-[ST]-[LIVMFY]-x-[LIVMFY](2)-x(3)-[DNS]-
                    [GS]-x(6)-[ED]-H
                    [H is a probable 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: June 1994 / Text revised.

[ 1] Berrard S., Brice A., Lottspeich F., Braun A., Barde Y.-A., Mallet J.
     Proc. Natl. Acad. Sci. U.S.A. 84:9280-9284(1987).
[ 2] Kispal G., Tomcsanyi T., Sumegi B., Bock I., Gajdos G., Dietmayer K.,
     Sandor A.
     J. Biol. Chem. 268:1824-1829(1993).
[ 3] Chatterjee B., Song C.S., Kim J.-M., Roy A.K.
     Biochemistry 27:9000-9006(1988).
[ 4] Esser V., Britton C.H., Weis B.C., Foster D.W., McGarry J.D.
     J. Biol. Chem. 268:5817-5822(1993).
[ 5] Schmalix W., Bandlow W.
     J. Biol. Chem. 268:27428-27439(1993).