HAMAP rule MF_00435

Accession	MF_00435
Dates	12-JUL-2001 (Created) 1-JUN-2023 (Last updated, Version 39)

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]

Triggered by

HAMAP; MF_00435 (Get profile general information and statistics)

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;

Protein name

AltName: Full=Ketol-acid reductoisomerase type 1; AltName: Full=Ketol-acid reductoisomerase type I;

Protein name

AltName: Full=Ketol-acid reductoisomerase type 2; AltName: Full=Ketol-acid reductoisomerase type II;

Gene name

ilvC

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.

Oxidoreductase
Amino-acid biosynthesis
Branched-chain amino acid biosynthesis
Magnesium
Metal-binding
NADP

Repeat

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.

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

From: ILVC_ECOLI (P05793)

Key

From

To

Description

Tag

Condition

FTGroup

BINDING (Optional)

45

48

/ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349

[CYF]-G-x-Q

BINDING (Optional)

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 (Optional)

68

68

/ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349

[RK]

BINDING (Optional)

76

76

/ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349

[RS]

BINDING (Optional)

78

78

/ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349

[ST]

BINDING (Optional)

158

158

/ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349

G

BINDING

414

414

/ligand="substrate

S

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.

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