ID ILVD_BACC3 Reviewed; 557 AA. AC C1EPL6; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 04-NOV-2026, entry version 80. DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012}; DE Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012}; GN Name=ilvD {ECO:0000255|HAMAP-Rule:MF_00012}; GN OrderedLocusNames=BCA_1859; OS Bacillus cereus (strain 03BB102). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=572264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=03BB102; RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C., RA Tapia R., Han C., Sutton G., Sims D.; RT "Genome sequence of Bacillus cereus 03BB102."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. 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 {ECO:0000255|HAMAP-Rule:MF_00012}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00012}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; 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:0000255|HAMAP-Rule:MF_00012}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis CC acid cofactor. {ECO:0000255|HAMAP-Rule:MF_00012}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00012}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001407; ACO26410.1; -; Genomic_DNA. DR RefSeq; WP_001255798.1; NC_012472.1. DR AlphaFoldDB; C1EPL6; -. DR SMR; C1EPL6; -. DR KEGG; bcx:BCA_1859; -. DR PATRIC; fig|572264.18.peg.1801; -. DR OMA; AADDHYS; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.50.30.80:FF:000001; Dihydroxy-acid dehydratase; 1. DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1. DR HAMAP; MF_00012; IlvD; 1. DR InterPro; IPR042096; Dihydro-acid_dehy_C. DR InterPro; IPR004404; DihydroxyA_deHydtase. DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS. DR InterPro; IPR056740; ILV_EDD_C. DR InterPro; IPR000581; ILV_EDD_N. DR InterPro; IPR037237; IlvD/EDD_N. DR NCBIfam; TIGR00110; ilvD; 1. DR NCBIfam; NF002068; PRK00911.1; 1. DR PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1. DR PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-RELATED; 1. DR Pfam; PF24877; ILV_EDD_C; 1. DR Pfam; PF00920; ILVD_EDD_N; 1. DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1. DR SUPFAM; SSF52016; LeuD/IlvD-like; 1. DR PROSITE; PS00886; ILVD_EDD_1; 1. DR PROSITE; PS00887; ILVD_EDD_2; 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..557 FT /note="Dihydroxy-acid dehydratase" FT /id="PRO_1000116499" FT ACT_SITE 468 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 78 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 119 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 120 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 121 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 192 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 442 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT MOD_RES 121 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" SQ SEQUENCE 557 AA; 59992 MW; 39AACA4DC2C3C30B CRC64; MRSDMIKKGF DKAPHRSLLK ATGLKDEDFD KPFIAICNSF IEIIPGHKHL NEFGKLVKEA VRAAGMVPFE FNTIGVDDGI AMGHIGMRYS LPSREIIADS VETVVNAHWF DGMICIPNCD KITPGMMMAA LRINIPTVFV SGGPMAAGKT SKGDVVDLSS VFEGVGAYQS GKISEEELKD IEDHGCPSCG SCSGMFTANS MNCLCEVLGL ALPGNGSILA IDPRREELIK QAAEKLKILI ERDIKPRDIV TEEAIDDAFA LDMAMGGSTN TVLHTLALAQ EAGLDYDMNR IDAVSRRVPH LCKVSPASNW HMEDIDRAGG ISAILKEMSR KEGVLHLDRI TATGQTLREN IAHAEIKDKE VIHSLENPHS EEGGLRILKG NLAKDGAVIK SGATEVKRFE GPCVIFNSQD EALAGIMLGK VKKGDVVVIR YEGPRGGPGM PEMLAPTSAI AGMGLGADVA LLTDGRFSGA SRGISVGHIS PEAAAGGTIA LLEQGDIVCI DVEERLLEVR VSDEELDKRK KEWKRPEPKV KTGWLGRYAQ MVTSANTGAV LKIPNFD //