HAMAP rule MF_01025
General rule information
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| Accession | MF_01025 |
| Dates | 5-JUL-2002 (Created)
25-APR-2024 (Last updated, Version 37) |
| Name | LeuA_type1 |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P09151 (LEU1_ECOLI); P15875 (LEU1_SALTY); Q9JZG1 (LEU1_NEIMB); P9WQB3 (LEU1_MYCTU); [ Recover all ] |
| Triggered by |
HAMAP; MF_01025 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | LEU1 |
| Protein name | RecName: Full=2-isopropylmalate synthase; EC=2.3.3.13; AltName: Full=Alpha-IPM synthase; AltName: Full=Alpha-isopropylmalate synthase; |
| Gene name | Name=leuA; |
Comments
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| FUNCTION | Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). |
| CATALYTIC ACTIVITY | Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2- isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13; |
| case <FTGroup:1> | |
| COFACTOR | Name=Mn(2+); Xref=ChEBI:CHEBI:29035; |
| end case | |
| PATHWAY | Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. |
| case <OC:Bacteria> | |
| SUBUNIT | Homodimer. |
| end case | |
| SIMILARITY | Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. |
Keywords
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| Amino-acid biosynthesis | |
| Branched-chain amino acid biosynthesis | |
| Cytoplasm | |
| Leucine biosynthesis | |
| case <FTGroup:1> | |
| Manganese | |
| Metal-binding | |
| end case | |
| Transferase | |
Gene Ontology
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| GO:0005737; Cellular component:cytoplasm | |
| case <FTGroup:1> | |
| GO:0030145; Molecular function:manganese ion binding | |
| end case | |
| GO:0003852; Molecular function:2-isopropylmalate synthase activity | |
| GO:0003985; Molecular function:acetyl-CoA C-acetyltransferase activity | |
| GO:0009098; Biological process:L-leucine biosynthetic process | |
Cross-references
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| Pfam | PF00682; HMGL-like; 1; |
| Pfam | PF08502; LeuA_dimer; 1; |
| NCBIfam | TIGR00973; leuA_bact; 1; |
| PROSITE | PS00815; AIPM_HOMOCIT_SYNTH_1; 1; |
| PROSITE | PS00816; AIPM_HOMOCIT_SYNTH_2; 1; |
| PROSITE | PS50991; PYR_CT; 1; |
Features
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| From: LEU1_NEIMB (Q9JZG1) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| REGION | 395 | Cter | /note="Regulatory domain" | |||||||||
| BINDING | 16 | 16 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" |
D | 1 | |||||||
| BINDING | 204 | 204 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" |
H | 1 | |||||||
| BINDING | 206 | 206 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" |
H | 1 | |||||||
| BINDING | 240 | 240 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" |
N | 1 | |||||||
Additional information
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| Size range | 350-600 amino acids |
| Related rules |
MF_00572 MF_01028 |
| Fusion | Nter: <Unknown> Cter: None |
| Comments | Shorter C-terminal in the two copies of leuA in CALS4; not shown in alignment and not taken into account in size range. Many Neisseria can be predicted to be about 80 residues longer. Salmonella typhimurium is thought to be in a monomer-tetramer equilibrium while Neisseria meningitidis and Mycobacterium tuberculosis (P9WQB3, MF_00572) are homodimers. |