AC   MF_00572;
DC   Protein; auto
TR   HAMAP; MF_00572; -; 1; level=0
XX
Names: LeuA_type2
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
end case
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily.
XX
DR   Pfam; PF00682; HMGL-like; 1; trigger=no
DR   Pfam; PF08502; LeuA_dimer; 1; trigger=no
DR   NCBIfam; TIGR00970; leuA_yeast; 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
KW   Transferase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0003852; F:2-isopropylmalate synthase activity
GO   GO:0003985; F:acetyl-CoA C-acetyltransferase activity
GO   GO:0009098; P:leucine biosynthetic process
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
XX
FT   From: LEU1_MYCTU (P9WQB3)
FT   REGION          491..Cter
FT                   /note="Regulatory domain"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: H
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: H
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: N
XX
Size: 530-675;
Related: MF_01025; MF_01028;
Template: P42455; P9WQB3;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in RALN1
Comments: Some Mycobacteria have variable number tandem repeats (VNTR)
 insertions in this gene; for example M.tuberculosis strains H37Rv and CDC 1551
 have 2 repeats, M.bovis strain ATCC BAA-935 / AF2122/97 has 5 repeats.
XX
# Revision 1.33 2023/11/28
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