{PDOC50979}
{PS50979; BC}
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* Biotin carboxylation (BC) domain profile *
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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 pyruvate or acetyl-CoA. The first step is mediated by the BC
domain  common  to all biotin-dependent carboxylases [1]. The BC domain can be
divided   in  three  subdomains  (N-terminal,  central  and  C-terminal).  The
N-terminal  region  provides  part  of  the  active  site;  the central region
corresponds to the ATP-grasp domain (see <PDOC50975>), which is common to many
ATP-dependent  enzymes involved in macromolecular synthesis [2]. The ATP-grasp
module  directly  binds the ATP molecule. The C-terminal subdomain is involved
in dimer formation.

Several  structure  of  the  BC  domain  have  been  solved  (see  for example
<PDB:1ULZ>)  [3,4].  The central module is splayed significantly away from the
main  body of the domain and is able to rotate of approximately 45 degree upon
nucleotide binding thereby closing off the active site pocket [4].

Enzymes known to contain a BC domain are listed below:

 - Pyruvate carboxylase (EC 6.4.1.1).
 - Acetyl-/propionyl-coenzyme A carboxylase alpha chain (EC 6.4.1.3).
 - Methylcrotonyl-CoA carboxylase alpha chain (EC 6.4.1.4).
 - Urea amidolyase (EC 6.3.4.6).
 - Acetyl-CoA carboxylase (EC 6.4.1.2).

The profile we developed covers the entire BC domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2004 / First entry.

[ 1] Jitrapakdee S., Wallace J.C.
     "The biotin enzyme family: conserved structural motifs and domain
     rearrangements."
     Curr. Protein. Pept. Sci. 4:217-229(2003).
     PubMed=12769720
[ 2] Artymiuk P.J., Poirrette A.R., Rice D.W., Willett P.
     "Biotin carboxylase comes into the fold."
     Nat. Struct. Biol. 3:128-132(1996).
     PubMed=8564538
[ 3] Kondo S., Nakajima Y., Sugio S., Yong-Biao J., Sueda S., Kondo H.
     "Structure of the biotin carboxylase subunit of pyruvate carboxylase
     from Aquifex aeolicus at 2.2 A resolution."
     Acta Crystallogr. D 60:486-492(2004).
     PubMed=14993673; DOI=10.1107/S0907444904000423
[ 4] Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L.
     "Movement of the biotin carboxylase B-domain as a result of ATP
     binding."
     J. Biol. Chem. 275:16183-16190(2000).
     PubMed=10821865; DOI=275/21/16183

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