ID ILVD_BACFR Reviewed; 600 AA. AC Q64PS6; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 107. 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}; OrderedLocusNames=BF3763; OS Bacteroides fragilis (strain YCH46). OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales; OC Bacteroidaceae; Bacteroides. OX NCBI_TaxID=295405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCH46; RX PubMed=15466707; DOI=10.1073/pnas.0404172101; RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.; RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions RT regulating cell surface adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004). 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; AP006841; BAD50505.1; -; Genomic_DNA. DR RefSeq; WP_011203429.1; NC_006347.1. DR AlphaFoldDB; Q64PS6; -. DR SMR; Q64PS6; -. DR STRING; 295405.BF3763; -. DR KEGG; bfr:BF3763; -. DR PATRIC; fig|295405.11.peg.3611; -. DR HOGENOM; CLU_014271_4_2_10; -. DR OrthoDB; 9807077at2; -. 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; NF009103; PRK12448.1; 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..600 FT /note="Dihydroxy-acid dehydratase" FT /id="PRO_0000225371" FT ACT_SITE 515 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 123 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 124 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 125 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 489 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT MOD_RES 125 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" SQ SEQUENCE 600 AA; 64371 MW; CE1C78D83FBD9302 CRC64; MKKQLRSSFS TQGRRMAGAR ALWAANGMKK EQLGKPIIAI VNSFTQFVPG HVHLHEIGQL VKKEIEKLGC FAAEFNTIAI DDGIAMGHDG MLYSLPSRDI IADSVEYMVN AHKADAMVCI SNCDKITPGM LMAAMRLNIP TVFVSGGPME AGELDGQHLD LIDAMIKSAD ESVSDEEVSK IENRACPTCG CCSGMFTANS MNCLNEAIGL ALPGNGTIVA THANRTQLFK DAAKQIVENT YKYYRDGDES VLPRSIATRE AFLNAMTLDI AMGGSTNTVL HLLAIAHEAE ADFKMDDIDM LSRKSPCLCK VAPNTQKYHI QDVNRAGGIM GIMGQLAKAG LIDTSVVRID GMTLGEAIDK YDITSPNVCE EAIKKYKSAA AGKFNLVLGS QDVYYKELDT DRAEGCIRDI EHAYSKDGGL AVLKGNIAQD GCVVKTAGVD ESIWKFTGPA KVFDSQEAAC NGILGGKVVS GDVVVITHEG PKGGPGMQEM LYPTSYIKSR HLGKECALIT DGRFSGGTSG LSIGHISPEA AAGGNIGKIK DGDIIEINIP ERTINVRLTD EELAARPMTP VTRERYVTKS LKAYASMVSS ADKGAVRLID //