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
IPR012846 is a Acetolactate synthase, large subunit, biosynthetic.
<p>Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this entry also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in Escherichia coli (strain K12), one of which contains a frameshift in the large subunit gene and is not expressed.</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 | Magnesium ion binding | Interacting selectively and non-covalently with magnesium (Mg) ions. | ||
Molecular function | Acetolactate synthase activity | Catalysis of the reaction: 2 pyruvate = 2-acetolactate + CO2. | ||
Biological process | Branched-chain amino acid biosynthetic process | The chemical reactions and pathways resulting in the formation of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine. | ||
Molecular function | Thiamine pyrophosphate binding | Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases. | ||
Molecular function | Flavin adenine dinucleotide binding | Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | Acetolactate synthase [Medicago littoralis] gi|164453114|gb|ABY57316.1| | 20 | ||
– | PREDICTED: acetolactate synthase 1, chloroplastic-like [Cicer arietinum] gi|502077817|ref|XP_004485753.1| | 20 | ||
– | Acetolactate synthase; TAIR: AT3G48560.1 chlorsulfuron/imidazolinone resistant 1; Swiss-Prot: sp|P09114|ILVB2_TOBAC Acetolactate synthase 2, chloroplastic; TrEMBL-Plants: tr|B0FBK4|B0FBK4_9FABA Acetolactate synthase; Found in the gene: LotjaGi1g1v0338500 | 21 | ||
– | Acetolactate synthase; TAIR: AT3G48560.1 chlorsulfuron/imidazolinone resistant 1; Swiss-Prot: sp|P09114|ILVB2_TOBAC Acetolactate synthase 2, chloroplastic; TrEMBL-Plants: tr|D2DJQ3|D2DJQ3_SOYBN Acetolactate synthase; Found in the gene: LotjaGi6g1v0333700 | 21 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
cd07035 | CDD | 1 | 25.00 |