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HAMAP rule MF_01025

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General rule information [?]

Accession MF_01025
Dates 5-JUL-2002 (Created)
1-JUN-2023 (Last updated, Version 36)
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 [?]

Identifier, protein and gene names [?]

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 [?]

FUNCTIONCatalyzes 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
PATHWAYAmino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
case <OC:Bacteria>
SUBUNITHomodimer.
end case
SIMILARITYBelongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.

Keywords [?]


Gene Ontology [?]

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:leucine biosynthetic process

Cross-references [?]

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 [?]

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 [?]

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.



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