|Function||acetolactate synthase, large subunit, biosynthetic type|
|Domain Trusted Cutoff||538.35|
|Domain Noise Cutoff||489.00|
|Mainrole Category||Amino acid biosynthesis|
|Subrole Category||Pyruvate family|
|Gene Ontology Term||GO:0003984: acetolactate synthase activity molecular_function|
| ||GO:0005948: acetolactate synthase complex cellular_component|
| ||GO:0009097: isoleucine biosynthetic process biological_process|
| ||GO:0009099: valine biosynthetic process biological_process|
|Entry Date||Apr 20 1999 2:06PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model 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 E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed.|
DR PROSITE; PDOC00166;
DR PFAM; PF00205; TPP_enzymes;
RT Cloning and phylogenetic analysis of the genes encoding acetohydroxyacid synthase from the archaeon Methanococcus aeolicus.
RT Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases.
RA Chipman D, Barak Z, Schloss JV;
RL Biochim Biophys Acta 1998 Jun 29;1385(2):401-19
AL clustalw, belvu
DR OUTGROUP; SP:P30146; glyoxylate carboligase; E. coli|
|Genome Property||GenProp0162: isoleucine biosynthesis from threonine and pyruvate (HMM)|
| ||GenProp0163: valine biosynthesis from pyruvate (HMM)|
| ||GenProp0164: leucine biosynthesis from pyruvate and acetyl-CoA (HMM)|
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