{PDOC50980}
{PS50980; COA_CT_NTER}
{PS50989; COA_CT_CTER}
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* Acetyl-coenzyme A carboxyltransferase domain profiles *
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Acetyl-coenzyme   A   carboxylase   (EC   6.4.1.2)  (ACC),  a  member  of  the
biotin-dependent  enzyme family, catalyses the formation of malonyl-coenzyme A
(CoA)  and  regulates  fatty acid biosynthesis and oxidation. Biotin-dependent
carboxylase  enzymes perform a two step reaction: enzyme-bound biotin is first
carboxylated  by  bicarbonate and ATP and the carboxyl group temporarily bound
to  biotin  is  subsequently  transferred  to  an  acceptor  substrate such as
acetyl-CoA.  The  carboxyltransferase  domain  perform  the second part of the
reaction [1,2].

The  N- and C-terminal regions of the carboxyltransferase domain share similar
polypeptide  backbone  folds,  with  a central beta-beta-alpha superhelix (see
<PDB:1OD2>)  [3].  The CoA molecule is mostly associated with the N subdomain.
In  bacterial acetyl coenzyme A carboxylase the N and C subdomains are encoded
by two different polypeptides.

The  acetyl-coenzyme  A  carboxyltransferase  domain  is  also  found  in  the
following enzymes:

 - Methylcrotonyl-CoA   carboxylase   beta   chain,   mitochondrial  precursor
   (EC 6.4.1.4).
 - Glutaconyl-CoA decarboxylase alpha subunit (EC 4.1.1.70).
 - Propionyl-CoA carboxylase beta chain (EC 6.4.1.3) (PCCase).

We  developed two profiles for this domain, one that spans the N subdomain and
also  recognizes the bacterial ACC beta-subunit, the other profile is directed
against  the  C  subdomain  and recognizes also the alpha-subunit of bacterial
ACC.

-Sequences known to belong to this class detected by the first profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the second profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: Herbicide  that  target  the   carboxyltransferase  domain are powerful
 inhibitors  of  plastid  ACC  and  can kill sensitive plants by shutting down
 fatty acid biosynthesis.

-Last update: August 2016 / Profiles revised.

[ 1] Knowles J.R.
     "The mechanism of biotin-dependent enzymes."
     Annu. Rev. Biochem. 58:195-221(1989).
     PubMed=2673009; DOI=10.1146/annurev.bi.58.070189.001211;
[ 2] Attwood P.V., Wallace J.C.
     "Chemical and catalytic mechanisms of carboxyl transfer reactions in
     biotin-dependent enzymes."
     Acc. Chem. Res. 35:113-120(2002).
     PubMed=11851389
[ 3] Zhang H., Yang Z., Shen Y., Tong L.
     "Crystal structure of the carboxyltransferase domain of
     acetyl-coenzyme A carboxylase."
     Science 299:2064-2067(2003).
     PubMed=12663926; DOI=10.1126/science.1081366

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