HAMAP rule MF_00435
General rule information
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| 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
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Identifier, protein and gene names
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| 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
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| 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 | 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 |
| PATHWAY | Amino-acid biosynthesis; L-isoleucine biosynthesis; L- isoleucine from 2-oxobutanoate: step 2/4. |
| PATHWAY | Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. |
| SIMILARITY | Belongs to the ketol-acid reductoisomerase family. |
Keywords
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| Oxidoreductase | |
| Amino-acid biosynthesis | |
| Branched-chain amino acid biosynthesis | |
| Magnesium | |
| Metal-binding | |
| NADP | |
| case <Feature:PS51851==2> | |
| Repeat | |
| end case | |
Gene Ontology
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| 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
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| 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
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| 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
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| 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. |