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PROSITE documentation PDOC00167

Biotin-requiring enzymes attachment site

Description:

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.

Note:

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>).

Last update:

December 2001 / Pattern and text revised.

Technical section:

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]

References:

1 AuthorsKnowles J.R.
TitleThe mechanism of biotin-dependent enzymes.
SourceAnnu. Rev. Biochem. 58:195-221(1989).
PubMed ID2673009
DOI10.1146/annurev.bi.58.070189.001211
2 AuthorsSamols D., Thornton C.G., Murtif V.L., Kumar G.K., Haase F.C., Wood H.G.
TitleEvolutionary conservation among biotin enzymes.
SourceJ. Biol. Chem. 263:6461-6464(1988).
PubMed ID2896195
3 AuthorsGoss N.H., Wood H.G.
TitleFormation of N epsilon-(biotinyl)lysine in biotin enzymes.
SourceMethods Enzymol. 107:261-278(1984).
PubMed ID6438443
4 AuthorsShenoy B.C., Xie Y., Park V.L., Kumar G.K., Beegen H., Wood H.G., Samols D.
TitleThe importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis.
SourceJ. Biol. Chem. 267:18407-18412(1992).
PubMed ID1526981

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