ILVD_CLOPA
ID ILVD_CLOPA Reviewed; 286 AA.
AC P31959;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Clostridium pasteurianum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1501;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8173074; DOI=10.3109/10425179309020149;
RA Oultram J.D., Loughlin M., Walmsley R.W., Gunnery S.M., Minton N.P.;
RT "The nucleotide sequence of genes involved in the leucine biosynthetic
RT pathway of Clostridium pasteurianum.";
RL DNA Seq. 4:105-111(1993).
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 EMBL; L06666; AAC41395.1; -; Genomic_DNA.
DR AlphaFoldDB; P31959; -.
DR SMR; P31959; -.
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 InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; SSF143975; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 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..>286
FT /note="Dihydroxy-acid dehydratase"
FT /id="PRO_0000103460"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 191
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT MOD_RES 121
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT NON_TER 286
SQ SEQUENCE 286 AA; 29926 MW; 7CF6665CC1EF5927 CRC64;
MRSDSARKGL EKAPHRSLFK ALGFIDEEME RPLIGIASSY SEIIPGHMNL DKVVQAVKDG
VRMAGGVPVT FGTIGVCDGI SMNHKGMSYS LPSRQLIADS VEIVASAHAF DGIVLVPNCD
KVVPGMMMAA ARLDIPAIVI SGGPMLAGNT CGKATDLSGV FEAVGAVKAG NMTEEELSEL
ENTACPTCGS CSGMYTANSM NCLSEVLGLA LPYNGTIPAV YSERLRLAKT SGMKIVDLVK
KGLTPSKILT EEAFMNAITA DMALGCSTNS LLHLPAIANE VGITID
