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Information on EC 1.1.1.382 - ketol-acid reductoisomerase (NAD+) and Organism(s) Ignisphaera aggregans and UniProt Accession E0SRA9

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IUBMB Comments
The enzyme, characterized from the bacteria Thermacetogenium phaeum and Desulfococcus oleovorans and from the archaeon Archaeoglobus fulgidus, is specific for NADH [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]].
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Ignisphaera aggregans
UNIPROT: E0SRA9
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The taxonomic range for the selected organisms is: Ignisphaera aggregans
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
ilvC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
(2R)-2,3-dihydroxy-3-methylbutanoate:NAD+ oxidoreductase (isomerizing)
The enzyme, characterized from the bacteria Thermacetogenium phaeum and Desulfococcus oleovorans and from the archaeon Archaeoglobus fulgidus, is specific for NADH [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme, to 1.39 A resolution, and in complex with NADP+. Enzyme accepts both cofactors NADH and NADPH. Insertions near the N-terminus of the specificity loop probably determine cofactor specificity, the laboratory engineering of NADH preference involved specific loop substitution
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cahn, J.K.; Brinkmann-Chen, S.; Spatzal, T.; Wiig, J.A.; Buller, A.R.; Einsle, O.; Hu, Y.; Ribbe, M.W.; Arnold, F.H.
Cofactor specificity motifs and the induced fit mechanism in Class I ketol-acid reductoisomerases
Biochem. J.
468
475-484
2015
Alicyclobacillus acidocaldarius subsp. acidocaldarius (C8WR67), Ignisphaera aggregans (E0SRA9), Ignisphaera aggregans DSM 17230 (E0SRA9), uncultured archaeon (Q64BR7), uncultured archaeon GZfos26G2 (Q64BR7)
Manually annotated by BRENDA team