ID   ILVD_RHOCA              Reviewed;          46 AA.
AC   P31874;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Dihydroxy-acid dehydratase;
DE            Short=DAD;
DE            EC=4.2.1.9 {ECO:0000250|UniProtKB:P9WKJ5};
DE   Flags: Fragment;
GN   Name=ilvD;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1319375; DOI=10.1016/0378-1097(92)90484-6;
RA   Kranz R.G., Beckman D.L., Foster-Hartnett D.;
RT   "DNA gyrase activities from Rhodobacter capsulatus: analysis of target(s)
RT   of coumarins and cloning of the gyrB locus.";
RL   FEMS Microbiol. Lett. 72:25-32(1992).
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       Is specific for the (R) isomer of 2,3-dihydroxy-3-methylbutanoate, with
CC       no catalytic activity against the (S) isomer.
CC       {ECO:0000250|UniProtKB:P9WKJ5}.
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         Evidence={ECO:0000250|UniProtKB:P9WKJ5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC         Evidence={ECO:0000250|UniProtKB:P9WKJ5};
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         Evidence={ECO:0000250|UniProtKB:P05791};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695;
CC         Evidence={ECO:0000250|UniProtKB:P05791};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P9WKJ5};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis
CC       acid cofactor. {ECO:0000250|UniProtKB:P9WKJ5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WKJ5};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4.
CC       {ECO:0000250|UniProtKB:P9WKJ5}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 3/4. {ECO:0000250|UniProtKB:P9WKJ5}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WKJ5}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000305}.
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DR   AlphaFoldDB; P31874; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   Pfam; PF00920; ILVD_EDD; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding.
FT   CHAIN           <1..>46
FT                   /note="Dihydroxy-acid dehydratase"
FT                   /id="PRO_0000103500"
FT   NON_TER         1
FT   NON_TER         46
SQ   SEQUENCE   46 AA;  5042 MW;  F1BE4CF8A3407737 CRC64;
     RTTEAFSTGN RYKEVDRDRQ AGVIRSAEHA FSKDGGLAVL FGNIAE