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HAMAP rule MF_00435

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General rule information [?]

Accession MF_00435
Dates 12-JUL-2001 (Created)
1-JUN-2023 (Last updated, Version 39)
Name IlvC
Scope(s) Bacteria
Archaea
Template(s) 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 ]
Triggered by HAMAP; MF_00435 (Get profile general information and statistics)

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 Name=ilvC;

Comments [?]

FUNCTIONInvolved 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 Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2- acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86;
CATALYTIC ACTIVITY Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2- ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit
PATHWAYAmino-acid biosynthesis; L-isoleucine biosynthesis; L- isoleucine from 2-oxobutanoate: step 2/4.
PATHWAYAmino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.
SIMILARITYBelongs to the ketol-acid reductoisomerase family.

Keywords [?]


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;
Pfam PF07991; IlvN; 1;
NCBIfam TIGR00465; IlvC; 1;
PROSITE PS51851; KARI_C; 1-2;
PROSITE PS51850; KARI_N; 1;

Features [?]

From: ILVC_ECOLI (P05793)
Key From To Description Tag Condition FTGroup
BINDING 45 48 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
[CYF]-G-x-Q
BINDING 108 110 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
D-x(1,2)-Q
ACT_SITE 132 132 H
BINDING 217 217 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"
D
BINDING 217 217 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
D
BINDING 221 221 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"
E
BINDING 389 389 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
E
BINDING 393 393 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
E
BINDING 68 68 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
[RK]
BINDING 76 76 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
[RS]
BINDING 78 78 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
[ST]
BINDING 158 158 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
G
BINDING 414 414 /ligand="substrate" S

Additional information [?]

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



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