EC Tree |
1. Oxidoreductases |
1.1 Acting on the CH-OH group of donors |
1.1.1 With NAD+ or NADP+ as acceptor |
ID: | 1.1.1.382 |
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Description: | Ketol-acid reductoisomerase (NAD(+)). |
Cath: | 1.10.1040.10; 1.10.3730.40; 3.40.50.720; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.1.1.382 |
BRENDA Enzyme Link: | BRENDA 1.1.1.382 |
KEGG Enzyme Link: | KEGG1.1.1.382 |
BioCyc Enzyme Link: | BioCyc 1.1.1.382 |
ExPASy Enzyme Link: | ExPASy1.1.1.382 |
EC2PDB Enzyme Link: | EC2PDB 1.1.1.382 |
ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.382 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.382 |
IntEnz Enzyme Link: | IntEnz 1.1.1.382 |
MEDLINE Enzyme Link: | MEDLINE 1.1.1.382 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:30627 | (2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-acetolactate + H(+) + NADH |
RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:4](-[*:5])(-[CH3;+0:6])-[OH;+0:7].[*:8]-[n+;H0:9]1:[cH;+0:10]:[cH;+0:11]:[cH;+0:12]:[c;H0;+0:13](-[*:14]):[cH;+0:15]:1>>[*:1]-[C;H0;+0:2](-[*:3])(-[CH3;+0:6])-[C;H0;+0:4](-[*:5])=[O;H0;+0:7].[*:8]-[N;H0;+0:9]1-[CH;+0:10]=[CH;+0:11]-[CH2;+0:12]-[C;H0;+0:13](-[*:14])=[CH;+0:15]-1 |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases. | Cahn JK, Brinkmann-Chen S, Buller AR, Arnold FH | 2016 Jul | 26644020 |
Uncovering rare NADH-preferring ketol-acid reductoisomerases. | Brinkmann-Chen S, Cahn JKB, Arnold FH | 2014 Nov | 25172159 |