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
IPR000506 is a Ketol-acid reductoisomerase, C-terminal.
<p>Ketol-acid reductoisomerase (KARI; ([ec:1.1.1.86])), also known as acetohydroxy acid isomeroreductase (AHIR or AHAIR), catalyzes the conversion of acetohydroxy acids into dihydroxy valerates in the second step of the biosynthetic pathway for the essential branched-chain amino acids valine, leucine, and isoleucine. KARI catalyzes an unusual two-step reaction consisting of an alkyl migration in which the substrate, either 2-acetolactate (AL) or 2-aceto-2-hydroxybutarate (AHB), is converted to 3-hydoxy-3-methyl-2- oxobutyrate or 3-hydoxy-3-methyl-2-pentatonate, followed by a NADPH-dependent reduction to give 2,3-dihydroxy-3-isovalerate or 2,3-dihydroxy-3- methylvalerate respectively [[cite:PUB00001302], [cite:PUB00088660], [cite:PUB00029172], [cite:PUB00034453], [cite:PUB00088661], [cite:PUB00088662]].</p> <p>KARI is present only in bacteria, fungi, and plants, but not in animals. KARIs are divided into two classes on the basis of sequence length and oligomerization state. Class I KARIs are ~340 amino acid residues in length and include all fungal KARIs, whereas class II KARIs are ~490 residues long and include all plant KARIs. Bacterial KARIs can be either class I or class II. KARIs are composed of two types of domains, an N-terminal Rossmann fold domain and one or two C-terminal knotted domains. Two intertwinned knotted domains are required for function, and in the short-chain or class I KARIs, each polypeptide chain has one knotted domain. As a result, dimerization of two monomers forms two complete KARI active sites. In the long-chain or class II KARIs, a duplication of the knotted domain has occurred and, as a result, the protein does not require dimerization to complete its active site [[cite:PUB00001302], [cite:PUB00088660], [cite:PUB00029172], [cite:PUB00034453], [cite:PUB00088661], [cite:PUB00088662]].</p> <p>The α-helical KARI C-terminal knotted domain can be described as a six- helix core in which helices coil like cable threads around each other, thus forming a bundle [[cite:PUB00001302], [cite:PUB00088660], [cite:PUB00029172], [cite:PUB00034453], [cite:PUB00088661]].</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 | Ketol-acid reductoisomerase activity | Catalysis of the reaction: (R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+. | ||
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. | ||
Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | Ketol-acid reductoisomerase [Medicago truncatula] gi|357474575|ref|XP_003607572.1| | 20 | ||
– | Ketol-acid reductoisomerase (NADP(+)); TAIR: AT3G58610.1 ketol-acid reductoisomerase; Swiss-Prot: sp|O82043|ILV5_PEA Ketol-acid reductoisomerase, chloroplastic; TrEMBL-Plants: tr|G7JCK0|G7JCK0_MEDTR Ketol-acid reductoisomerase; Found in the gene: LotjaGi3g1v0247900 | 24 | ||
– | Ketol-acid reductoisomerase (NADP(+)); TAIR: AT3G58610.1 ketol-acid reductoisomerase; Swiss-Prot: sp|O82043|ILV5_PEA Ketol-acid reductoisomerase, chloroplastic; TrEMBL-Plants: tr|G7JCK0|G7JCK0_MEDTR Ketol-acid reductoisomerase; Found in the gene: LotjaGi3g1v0247900 | 16 | ||
– | Ketol-acid reductoisomerase (NADP(+)); TAIR: AT3G58610.1 ketol-acid reductoisomerase; Swiss-Prot: sp|O82043|ILV5_PEA Ketol-acid reductoisomerase, chloroplastic; TrEMBL-Plants: tr|G7JCK0|G7JCK0_MEDTR Ketol-acid reductoisomerase; Found in the gene: LotjaGi3g1v0247900 | 19 | ||
– | Ketol-acid reductoisomerase; TAIR: AT3G58610.1 ketol-acid reductoisomerase; Swiss-Prot: sp|O82043|ILV5_PEA Ketol-acid reductoisomerase, chloroplastic; TrEMBL-Plants: tr|G7JCK0|G7JCK0_MEDTR Ketol-acid reductoisomerase; Found in the gene: LotjaGi3g1v0247900 | 10 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
SSF48179 | SUPERFAMILY | 1 | 20.00 |