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Annotation rule MF_00435
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General rule information [?]

Accession MF_00435
Dates 12-JUL-2001 (Created)
18-NOV-2019 (Last updated, Version 36)
Name IlvC
Scope
Bacteria
Archaea
Templates P05793 (ILVC_ECOLI); Q57179 (ILVC_CORGL); P05989 (ILVC_SALTY); D0WGK0 (ILVC_SLAES); K4LVZ1 (ILVC_THEPS); Q0AV19 (ILVC_SYNWW); B4U6I9 (ILVC_HYDS0); C1DFH7 (ILVC_AZOVD); C8WR67 (ILVC_ALIAD); Q02138 (ILVC_LACLA); P9WKJ7 (ILVC_MYCTU); E0SRA9 (ILVC_IGNAA); O28294 (ILVC_ARCFU); A4YI15 (ILVC_METS5); Q64BR7 (ILVC_UNCAG): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
ILVC
Protein name
RecName: Full=Ketol-acid reductoisomerase (NADP(+));
Short=KARI;
EC 1.1.1.86;
AltName: Full=Acetohydroxy-acid isomeroreductase;
Short=AHIR;
AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
case <Feature:PS51851==1>
Protein name
AltName: Full=Ketol-acid reductoisomerase type 1;
AltName: Full=Ketol-acid reductoisomerase type I;
else case <Feature:PS51851==2>
Protein name
AltName: Full=Ketol-acid reductoisomerase type 2;
AltName: Full=Ketol-acid reductoisomerase type II;
end case
Gene name
ilvC

Comments [?]

Function Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic activity RHEA:22068: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
EC 1.1.1.86
RHEA:13493: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH
EC 1.1.1.86
Cofactor Mg(2+)
Note: Binds 2 magnesium ions per subunit
Pathway Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.
Similarity Belongs to the ketol-acid reductoisomerase family.

Keywords [?]

case <Feature:PS51851==2>
end case

Gene Ontology [?]

GO:0000287; Molecular function: magnesium ion binding.
GO:0004455; Molecular function: ketol-acid reductoisomerase activity.
GO:0009097; Biological process: isoleucine biosynthetic process.
GO:0009099; Biological process: valine biosynthetic process.

Cross-references [?]

Pfam PF01450; IlvC; 1-2;
PF07991; IlvN; 1;
TIGRFAMs TIGR00465; IlvC; 1;
PROSITE PS51851; KARI_C; 1-2; trigger=PRU01198;
PS51850; KARI_N; 1; trigger=PRU01197;

Features [?]

From: ILVC_ECOLI (P05793)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND (Optional)     45     48       NADP     [CYF]-G-x-Q  
NP_BIND (Optional)     108     110       NADP     D-x(1,2)-Q  
ACT_SITE     132     132             H  
METAL     217     217       Magnesium 1     D  
METAL     217     217       Magnesium 2     D  
METAL     221     221       Magnesium 1     E  
METAL     389     389       Magnesium 2     E  
METAL     393     393       Magnesium 2     E  
BINDING (Optional)     68     68       NADP     [RK]  
BINDING (Optional)     76     76       NADP     [RS]  
BINDING (Optional)     78     78       NADP     [ST]  
BINDING (Optional)     158     158       NADP; via amide nitrogen     G  
BINDING     414     414       Substrate     S  

Additional information [?]

Size range 326-494 amino acids
Related rules None
Fusion None
Comments Two additional divergent sequences in SACS2 (SSO1322 and SSO1942) not shown in alignment. Enterobacteria have a duplication of the KARI_C domain.