ID ILVD_THEFY Reviewed; 625 AA. AC Q47MS7; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 02-SEP-2026, entry version 119. 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=Tfu_2209; OS Thermobifida fusca (strain YX). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales; OC Nocardiopsidaceae; Thermobifida. OX NCBI_TaxID=269800; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YX; RX PubMed=17209016; DOI=10.1128/jb.01899-06; RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., RA Kyrpides N.; RT "Genome sequence and analysis of the soil cellulolytic actinomycete RT Thermobifida fusca YX."; RL J. Bacteriol. 189:2477-2486(2007). 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; CP000088; AAZ56242.1; -; Genomic_DNA. DR RefSeq; WP_011292632.1; NC_007333.1. DR AlphaFoldDB; Q47MS7; -. DR SMR; Q47MS7; -. DR STRING; 269800.Tfu_2209; -. DR KEGG; tfu:Tfu_2209; -. DR eggNOG; COG0129; Bacteria. DR HOGENOM; CLU_014271_4_2_11; -. 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..625 FT /note="Dihydroxy-acid dehydratase" FT /id="PRO_0000225432" FT ACT_SITE 522 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 81 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 122 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 123 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 124 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 199 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 496 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT MOD_RES 124 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" SQ SEQUENCE 625 AA; 65802 MW; 70685FC7EDE06ACE CRC64; MPALRSRTVT HGRNMAGARA LLRATGVARE DFGKPIVAVA NSYTQFVPGH VHLREVADVV ADAVRAAGGV PREFNTIAVD DGIAMGHGGM LYSLPSRELI ADAVEYMVNA HCADALVCVS NCDKITPGML LAALRLNIPT VFVSGGPMEA GKVTVVNGTA TTVRKLDLIN PMIASADENV SEQELNALEE AACPTCGSCS GMFTANSMNC LTEAIGLALP GNGTVLATHT ARKKLYEEAG RVVVEAARRY YEKDDESVLP LSIATPAAFA NAMALDVAMG GSTNTILHLL AAATEAGVDF GLDDIDALSR RVPCLCKVAP NSDKYHIEDV HRAGGIPAIM GELARAGLVD TSLPMVHGMT VGEYVDAWDI ASPNVRPEAV ELFHAAPGGQ RSTEAFSQST RWDSLDLDRE SGCIRSVKHA YTKDGGLAVL KGNLAPDGAV VKTAGVDEEL WTFSGPAKVF ESQEEAVDGI LNKAVQPGDV VVIRYEGPKG GPGMQEMLYP TSFLKGRGLG KVCALITDGR FSGGTSGLSI GHASPEAAAG GDIALVEDGD IITIDIPNRS ITLEVPEDEL NARRERLLKE LGGFRPRNRQ RPVSAALRAY AAMATSASTG AARDVSQVER THLHS //