AC   MF_01027;
DC   Protein; auto
TR   HAMAP; MF_01027; -; 1; level=0
XX
Names: LeuC_type2
XX
ID   LEUC
DE   RecName: Full=3-isopropylmalate dehydratase large subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuC;
XX
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC         Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC         EC=4.2.1.33;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC       subfamily.
XX
DR   Pfam; PF00330; Aconitase; 1; trigger=no
DR   PRINTS; PR00415; ACONITASE; 1; trigger=no
DR   NCBIfam; TIGR01343; hacA_fam; 1; trigger=no
DR   NCBIfam; TIGR02086; IPMI_arch; 1; trigger=no
DR   NCBIfam; TIGR02083; LEU2; 1; trigger=no
DR   PROSITE; PS00450; ACONITASE_1; 1; trigger=no
DR   PROSITE; PS01244; ACONITASE_2; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Branched-chain amino acid biosynthesis
KW   Leucine biosynthesis
KW   Lyase
KW   Metal-binding
KW   Iron
KW   Iron-sulfur
KW   4Fe-4S
XX
GO   GO:0003861; F:3-isopropylmalate dehydratase activity
GO   GO:0009098; P:leucine biosynthetic process
XX
FT   From: LEUC_AQUAE (O67078)
FT   BINDING         299
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Condition: C
FT   BINDING         364
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Condition: C
FT   BINDING         367
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Condition: C
XX
Size: 380-434;
Related: MF_01026;
Template: P0A6A6; P15717;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARCFU, DEIRA, METAC, METJA, METKA, METMA, METTH, PYRAB, PYRFU,
 THEMA
Plasmid: 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).
XX
# Revision 1.40 2023/06/01
//