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Annotation rule MF_01027
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General rule information [?]

Accession MF_01027
Dates 17-JUL-2002 (Created)
19-NOV-2019 (Last updated, Version 37)
Name LeuC_type2
Scope
Bacteria
Archaea
Templates P0A6A6 (LEUC_ECOLI); P15717 (LEUC1_SALTY): [Recover all]

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
leuC

Comments [?]

Function Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic activity RHEA:32287: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
EC 4.2.1.33
Cofactor [4Fe-4S] cluster
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 [?]


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;
TIGRFAMs TIGR01343; hacA_fam; 1;
TIGR02086; IPMI_arch; 1;
TIGR02083; LEU2; 1;
PROSITE PS00450; ACONITASE_1; 1;
PS01244; ACONITASE_2; 1;

Features [?]

From: LEUC_AQUAE (O67078)
Key     From     To       Description   Tag   Condition   FTGroup
METAL     299     299       Iron-sulfur (4Fe-4S)     C  
METAL     364     364       Iron-sulfur (4Fe-4S)     C  
METAL     367     367       Iron-sulfur (4Fe-4S)     C  

Additional information [?]

Size range 380-434 amino acids
Related rules MF_01026 (LEUC)
Fusion 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).