HAMAP rule MF_01025

General rule information [?]

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

Name	LeuA_type1

Scope

Bacteria

Archaea

Templates

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

leuA

Comments [?]

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	RHEA:21524: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+) EC 2.3.3.13

case <FTGroup:1>

Cofactor

Mn(2+)

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 [?]

Amino-acid biosynthesis
Branched-chain amino acid biosynthesis
Cytoplasm
Leucine biosynthesis

case <FTGroup:1>

Manganese
Metal-binding

end case

Transferase

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;
	PF08502; LeuA_dimer; 1;
NCBIfam	TIGR00973; leuA_bact; 1;
PROSITE	PS00815; AIPM_HOMOCIT_SYNTH_1; 1;
	PS00816; AIPM_HOMOCIT_SYNTH_2; 1;
	PS50991; PYR_CT; 1; trigger=PRU01151;

Features [?]

From: LEU1_NEIMB (Q9JZG1)

Key From To Description Tag Condition FTGroup

REGION 395 Cter 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 (LEU1); MF_01028 (CIMA supersedes the current rule)
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.

View rule in raw text format (no links)