HAMAP rule MF_01027
General rule information
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Accession | MF_01027 |
Dates | 17-JUL-2002 (Created)
1-JUN-2023 (Last updated, Version 40) |
Name | LeuC_type2 |
Scope(s) |
Bacteria Archaea |
Template(s) | P0A6A6 (LEUC_ECOLI); P15717 (LEUC1_SALTY); [ Recover all ] |
Triggered by |
HAMAP; MF_01027 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | LEUC |
Protein name | RecName: Full=3-isopropylmalate dehydratase large subunit; EC=4.2.1.33; AltName: Full=Alpha-IPM isomerase; Short=IPMI; AltName: Full=Isopropylmalate isomerase; |
Gene name | Name=leuC; |
Comments
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FUNCTION | Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. |
CATALYTIC ACTIVITY | Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate; Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121; EC=4.2.1.33; |
COFACTOR | Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.; |
PATHWAY | Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. |
SUBUNIT | Heterodimer of LeuC and LeuD. |
SIMILARITY | Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily. |
Keywords
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Amino-acid biosynthesis |
Branched-chain amino acid biosynthesis |
Leucine biosynthesis |
Lyase |
Metal-binding |
Iron |
Iron-sulfur |
4Fe-4S |
Gene Ontology
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GO:0003861; Molecular function:3-isopropylmalate dehydratase activity |
GO:0009098; Biological process:leucine biosynthetic process |
Cross-references
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Pfam | PF00330; Aconitase; 1; |
PRINTS | PR00415; ACONITASE; 1; |
NCBIfam | TIGR01343; hacA_fam; 1; |
NCBIfam | TIGR02086; IPMI_arch; 1; |
NCBIfam | TIGR02083; LEU2; 1; |
PROSITE | PS00450; ACONITASE_1; 1; |
PROSITE | PS01244; ACONITASE_2; 1; |
Features
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From: LEUC_AQUAE (O67078) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 299 | 299 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | ||||||||
BINDING | 364 | 364 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | ||||||||
BINDING | 367 | 367 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C |
Additional information
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Size range | 380-434 amino acids |
Related rules |
MF_01026 |
Fusion | Nter: None Cter: None |
Comments | The family member in THET2 is shown to function as a homoaconitase (for lysine biosynthesis), as well as one of the 2 copies found in METJA that catalyzes both the dehydration of (R)-homocitrate and the hydration of cis-homoaconitate for coenzyme B biosynthesis. The other copy in METJA functions both in leucine and isoleucine biosynthesis, since it catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate and between 2-methylmalate and 3-methylmalate. It seems to be impossible to automatically distinguish the large subunit of homoaconitase (HacA) from that of 3-isopropylmalate dehydratase (LeuC). |