AC   MF_01025;
DC   Protein; auto
TR   HAMAP; MF_01025; -; 1; level=0
XX
Names: LeuA_type1
XX
ID   LEU1
DE   RecName: Full=2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
GN   Name=leuA;
XX
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-
CC       hydroxy-4-methylpentanoate (2-isopropylmalate).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
end case
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
case <OC:Bacteria>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily.
XX
DR   Pfam; PF00682; HMGL-like; 1; trigger=no
DR   Pfam; PF08502; LeuA_dimer; 1; trigger=no
DR   NCBIfam; TIGR00973; leuA_bact; 1; trigger=no
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1; trigger=no
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1; trigger=no
DR   PROSITE; PS50991; PYR_CT; 1; trigger=yes
XX
KW   Amino-acid biosynthesis
KW   Branched-chain amino acid biosynthesis
KW   Cytoplasm
KW   Leucine biosynthesis
case <FTGroup:1>
KW   Manganese
KW   Metal-binding
end case
KW   Transferase
XX
GO   GO:0005737; C:cytoplasm
case <FTGroup:1>
GO   GO:0030145; F:manganese ion binding
end case
GO   GO:0003852; F:2-isopropylmalate synthase activity
GO   GO:0003985; F:acetyl-CoA C-acetyltransferase activity
GO   GO:0009098; P:leucine biosynthetic process
XX
FT   From: LEU1_NEIMB (Q9JZG1)
FT   REGION          395..Cter
FT                   /note="Regulatory domain"
FT   BINDING         16
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Group: 1; Condition: D
FT   BINDING         204
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Group: 1; Condition: H
FT   BINDING         206
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Group: 1; Condition: H
FT   BINDING         240
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Group: 1; Condition: N
XX
Size: 350-600;
Related: MF_00572; MF_01028!;
Template: P09151; P15875; Q9JZG1; P9WQB3;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <Unknown>
 Cter: None
Duplicate: in CALS4
Plasmid: in BUCAI, BUCAP, BUCDN, BUCML, BUCRP, BUCTS, BUCUE, BUCUL, BUCUM, BUCUN
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.
XX
# Revision 1.36 2023/06/01
//