Structural classification of biotin carboxyl carrier proteins

Abstract

We gathered primary and tertiary structures of acyl-CoA carboxylases from public databases, and established that members of their biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains occur in one family each and that members of their carboxyl transferase (CT) domains occur in two families. Protein families have members similar in primary and tertiary structure that probably have descended from the same protein ancestor. The BCCP domains complexed with biotin in acyl and acyl-CoA carboxylases transfer bicarbonate ions from BC domains to CT domains, enabling the latter to carboxylate acyl and acyl-CoA moieties. We separated the BCCP domains into four subfamilies based on more subtle primary structure differences. Members of different BCCP subfamilies often are produced by different types of organisms and are associated with different carboxylases. KeywordsAcyl-CoA carboxylase, Biotin, carboxylase carrier protein, primary structure, protein families, tertiary structure, ThYme domains, enabling the latter to carboxylate acyl and acyl-CoA moieties. We separated the BCCP domains into four subfamilies based on more subtle primary structure differences.Members of different BCCP subfamilies often are produced by different types of organisms and are associated with different carboxylases.

Genome-Wide Identification and Expression Analysis of the Biotin Carboxyl Carrier Subunits of Heteromeric Acetyl-CoA Carboxylase in Gossypium

“…Among the subunits of heteromeric ACCase, BCCP subunit interacts with BC and accepts a bicarbonate ion when ATP is converted to ADP, thus it can be served as the donor of activated carboxyl group, then the complex (BCCP-biotin) transfers the ion to CT, and finally produces malonyl-CoA in fatty acid biosynthesis (Ke et al, 2000; Sasaki and Nagano, 2004; Chen et al, 2012; Jang et al, 2015). Previous studies revealed that BCCP subunits have variable protein lengths, and low similarity (Qiao and Liu, 2007), while each of BCCP subunits contains a biotinylated domain located at the C-terminal region, harboring a highly conserved motif (CIIEAMKLMNEIE) (Qiao and Liu, 2007; Xuan et al, 2015).…”

Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity

“…The BCCP domain physically translocates between catalytic domains and assists in inserting biotin into the individual active sites. The primary sequence and tertiary structure for the C-terminal ∼80 amino acids of the BCCP domain is conserved for all enzymes within the family, suggesting that they are descended from a common ancestor [20]. In Escherichia coli acetyl-CoA carboxylase, however, the BCCP subunit includes an additional N-terminal domain of ∼80 amino acids which may serve to impede the catalytic half-reactions prior to assembly of the complete enzyme complex [21], [22].…”

Legume Cytosolic and Plastid Acetyl-Coenzyme—A Carboxylase Genes Differ by Evolutionary Patterns and Selection Pressure Schemes Acting before and after Whole-Genome Duplications

“…The Papilionoideae plastid ACCase consists of four subunits, each coded by a separate gene: biotin carboxylase (BC, gene accC ), biotin carboxyl carrier protein (BCCP, gene accB ), alpha-carboxyltransferase (a-CT, gene accA ) and beta-carboxyltransferase (b-CT, gene accD ). The genes coding three of these subunits: accC , accB , and accA , are localized in the nuclear genome whereas accD gene is localized in the plastid genome [ 51 , 52 ]. This type of enzyme forms active complex inside plastids and is named heteromeric (ht) ACCase or bacterial type ACCase.…”