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Biotin, which plays a catalytic role in some carboxyl transfer reactions, is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme [1,2,3,4]. Such enzymes are:

• Pyruvate carboxylase (EC 6.4.1.1).
• Acetyl-CoA carboxylase (EC 6.4.1.2).
• Propionyl-CoA carboxylase (EC 6.4.1.3).
• Methylcrotonyl-CoA carboxylase (EC 6.4.1.4).
• Geranoyl-CoA carboxylase (EC 6.4.1.5).
• Urea carboxylase (EC 6.3.4.6).
• Oxaloacetate decarboxylase (EC 4.1.1.3).
• Methylmalonyl-CoA decarboxylase (EC 4.1.1.41).
• Glutaconyl-CoA decarboxylase (EC 4.1.1.70).
• Methylmalonyl-CoA carboxyl-transferase (EC 2.1.3.1) (transcarboxylase).

Sequence data reveal that the region around the biocytin (biotin-lysine) residue is well conserved and can be used as a signature pattern.

The domain around the biotin-binding lysine residue is evolutionary related to that around the lipoyl-binding lysine residue of 2-oxo acid dehydrogenase acyltransferases (see <PDOC00168>).

December 2001 / Pattern and text revised.

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

BIOTIN, PS00188; Biotin-requiring enzymes attachment site  (PATTERN)

Consensus pattern: [GDN]-[DEQTR]-x-[LIVMFY]-x(2)-[LIVM]-x-[AIV]-M-K-[LVMAT]-x(3)-[LIVM]-x-[SAV] K is the biotin attachment site Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• 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 PS00188 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00188 • Scan Swiss-Prot/TrEMBL entries against PS00188 • view ligand binding statistics

Matching PDB structures: 1A6X 1BDO 1DCZ 1DD2 ... [ALL]

1	Authors	Knowles J.R.
	Title	The mechanism of biotin-dependent enzymes.
	Source	Annu. Rev. Biochem. 58:195-221(1989).
	PubMed ID	2673009
	DOI	10.1146/annurev.bi.58.070189.001211

2	Authors	Samols D., Thornton C.G., Murtif V.L., Kumar G.K., Haase F.C., Wood H.G.
	Title	Evolutionary conservation among biotin enzymes.
	Source	J. Biol. Chem. 263:6461-6464(1988).
	PubMed ID	2896195

3	Authors	Goss N.H., Wood H.G.
	Title	Formation of N epsilon-(biotinyl)lysine in biotin enzymes.
	Source	Methods Enzymol. 107:261-278(1984).
	PubMed ID	6438443

4	Authors	Shenoy B.C., Xie Y., Park V.L., Kumar G.K., Beegen H., Wood H.G., Samols D.
	Title	The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis.
	Source	J. Biol. Chem. 267:18407-18412(1992).
	PubMed ID	1526981

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