AC   MF_00012;
DC   Protein; auto
TR   HAMAP; MF_00012; -; 1; level=0
XX
Names: IlvD
XX
ID   ILVD
DE   RecName: Full=Dihydroxy-acid dehydratase;
DE            Short=DAD;
DE            EC=4.2.1.9;
GN   Name=ilvD;
XX
CC   -!- FUNCTION: Functions in the biosynthesis of branched-chain amino acids.
CC       Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate
CC       (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-
CC       3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-
CC       dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate),
CC       the penultimate precursor to L-isoleucine and L-valine, respectively.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate
CC         + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:49072; EC=4.2.1.9;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-
CC         oxopentanoate + H2O; Xref=Rhea:RHEA:27694, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:35146, ChEBI:CHEBI:49258; EC=4.2.1.9;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis
CC       acid cofactor.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 3/4.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
XX
DR   Pfam; PF00920; ILVD_EDD; 1; trigger=no
DR   NCBIfam; TIGR00110; IlvD; 1; trigger=no
DR   PROSITE; PS00886; ILVD_EDD_1; 1; trigger=no
DR   PROSITE; PS00887; ILVD_EDD_2; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Branched-chain amino acid biosynthesis
KW   Lyase
KW   Metal-binding
KW   Iron
KW   Iron-sulfur
KW   2Fe-2S
KW   Magnesium
XX
GO   GO:0000287; F:magnesium ion binding
GO   GO:0004160; F:dihydroxy-acid dehydratase activity
GO   GO:0051537; F:2 iron, 2 sulfur cluster binding
GO   GO:0009097; P:isoleucine biosynthetic process
GO   GO:0009099; P:valine biosynthetic process
XX
FT   From: ILVD_MYCTU (P9WKJ5)
FT   ACT_SITE        491
FT                   /note="Proton acceptor"
FT   Condition: S
FT   BINDING         64
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Optional; Condition: C
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         122
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Condition: C
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT   Condition: K
FT   BINDING         195
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Condition: C
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: E
FT   MOD_RES         139
FT                   /note="N6-carboxylysine"
FT   Condition: K
XX
Size: 547-629;
Related: None;
Template: P05791; P9WKJ5;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BORBR, BORPA, BORPE, BRADU, COREF, RHILO
Plasmid: None
Comments: None
XX
# Revision 1.39 2023/06/01
//