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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 α chain (EC 6.4.1.3).
• Methylcrotonyl-CoA carboxylase α 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.

April 2004 / First entry.

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

BC, PS50979; Biotin carboxylation domain profile  (MATRIX)

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

• Domain architecture view of Swiss-Prot proteins matching PS50979 • 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 PS50979 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50979 • Scan Swiss-Prot/TrEMBL entries against PS50979 • view ligand binding statistics

Matching PDB structures: 1BNC 1DV1 1DV2 1K69 ... [ALL]

1	Authors	Jitrapakdee S., Wallace J.C.
	Title	The biotin enzyme family: conserved structural motifs and domain rearrangements.
	Source	Curr. Protein. Pept. Sci. 4:217-229(2003).
	PubMed ID	12769720

2	Authors	Artymiuk P.J., Poirrette A.R., Rice D.W., Willett P.
	Title	Biotin carboxylase comes into the fold.
	Source	Nat. Struct. Biol. 3:128-132(1996).
	PubMed ID	8564538

3	Authors	Kondo S., Nakajima Y., Sugio S., Yong-Biao J., Sueda S., Kondo H.
	Title	Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution.
	Source	Acta Crystallogr. D 60:486-492(2004).
	PubMed ID	14993673
	DOI	10.1107/S0907444904000423

4	Authors	Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L.
	Title	Movement of the biotin carboxylase B-domain as a result of ATP binding.
	Source	J. Biol. Chem. 275:16183-16190(2000).
	PubMed ID	10821865
	DOI	275/21/16183

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