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HAMAP rule MF_01027

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General rule information [?]

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 [?]

Identifier, protein and gene names [?]

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 [?]

FUNCTIONCatalyzes 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.;
PATHWAYAmino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
SUBUNITHeterodimer of LeuC and LeuD.
SIMILARITYBelongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.

Keywords [?]


Gene Ontology [?]

GO:0003861; Molecular function:3-isopropylmalate dehydratase activity
GO:0009098; Biological process:leucine biosynthetic process

Cross-references [?]

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 [?]

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 [?]

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).



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