Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR004408 is a Biotin--acetyl-CoA-carboxylase ligase.
<p>The biotin operon of Escherichia coli contains 5 structural genes involved in the synthesis of biotin. Transcription of the operon is regulated via one of these proteins, the biotin ligase BirA. BirA is an asymetric protein with 3 specific domains -an N-terminal DNA-binding domain, a central catalytic domain and a C-terminal of unknown function. The ligase reaction intermediate, biotinyl-5'-AMP, is the co-repressor that triggers DNA binding by BirA. The α-helical N-terminal domain of the BirA protein has the helix-turn-helix structure of DNA-binding proteins with a central DNA recognition helix. BirA undergoes several conformational changes related to repressor function and the N-terminal DNA-binding function is connected to the rest of the molecule through a hinge which will allow relocation of the domains during the reaction [[cite:PUB00005496]]. Biotin-binding causes a large structural change thought to facilitate ATP-binding.</p> <p>Two repressor molecules form the operator-repressor complex, with dimer formation occuring simultaneously with DNA binding. DNA-binding may also cause a conformational change which allows this co-operative interaction. In the dimer structure, the β-sheets in the central domain of each monomer are arranged side-by-side to form a single, seamless β-sheet.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Biotin-[acetyl-CoA-carboxylase] ligase activity | Catalysis of the reaction: ATP + biotin + apo-(acetyl-CoA:carbon-dioxide ligase (ADP forming)) = AMP + diphosphate + (acetyl-CoA:carbon-dioxide ligase (ADP forming)). | ||
| Biological process | Cellular protein modification process | The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: biotin--protein ligase-like [Cicer arietinum] gi|502130276|ref|XP_004500594.1| | 7 | ||
| – | Holocarboxylase synthetase hcs2 [Medicago truncatula] gi|357461633|ref|XP_003601098.1| | 4 | ||
| – | Holocarboxylase synthetase hcs2 [Medicago truncatula] gi|357461633|ref|XP_003601098.1| | 12 | ||
| – | Biotin holocarboxylase synthetase 1-like protein; TAIR: AT2G25710.1 holocarboxylase synthase 1; Swiss-Prot: sp|Q9SL92|HCS1_ARATH Biotin--protein ligase 1, chloroplastic; TrEMBL-Plants: tr|G7J3L5|G7J3L5_MEDTR Biotin holocarboxylase synthetase, putative; Found in the gene: LotjaGi1g1v0254100 | 12 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd16442 | CDD | 1 | 25.00 |