ID ILVD_KOCRD Reviewed; 612 AA. AC B2GLR9; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 02-SEP-2026, entry version 90. 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=KRH_02560; OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Micrococcaceae; Kocuria. OX NCBI_TaxID=378753; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201; RX PubMed=18408034; DOI=10.1128/jb.01853-07; RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila."; RL J. Bacteriol. 190:4139-4146(2008). 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; AP009152; BAG28603.1; -; Genomic_DNA. DR RefSeq; WP_012397330.1; NC_010617.1. DR AlphaFoldDB; B2GLR9; -. DR SMR; B2GLR9; -. DR STRING; 378753.KRH_02560; -. DR KEGG; krh:KRH_02560; -. DR eggNOG; COG0129; Bacteria. DR HOGENOM; CLU_014271_4_3_11; -. DR OrthoDB; 9807077at2; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000008838; Chromosome. 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; Reference proteome. FT CHAIN 1..612 FT /note="Dihydroxy-acid dehydratase" FT /id="PRO_1000089392" FT ACT_SITE 518 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 195 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 492 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 612 AA; 64991 MW; 7CB99F6FB1614500 CRC64; MPQLRSATST TGRNMAGARA LWRATGMGSE DFGKPIVAIA NSFTQFVPGH VHLKNMGELV ASAVQEAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSRDII ADSVEYMVNA HCADALVCIS NCDKITPGML MAALRLNIPV VFVSGGPMES GEGVEGVVEH RVDLVDAMSL AVDESVTDAQ LAQIEENACP TCGSCSGMFT ANSMNCLTEA LGLSLPGNGT TLATHVNRKR LFLEAGRRAV ESAKKYYEQD DESVLPRSIA TKAAFENAMA LDIAMGGSTN TVLHILAAAQ EAEVDFNLSD IDALSRQVPC LAKVAPNSTT FHIEHVHRAG GIPAILGELR RGGLLNEDVH TVHSQTMGEW LDEWDIRSGK ASDAAKEFFL AAPGGVRTTQ AFSQANEYED HDVDAAGGCI RSVEHAYTKE GGLCVLFGNI AEDGAVIKTA GIDPELFHFT GRAFVVESQD EAVHEILSKN VKEGDIVVIA YEGPKGGPGM QEMLYPTSYL KGLGLGKKCA LITDGRFSGG TSGLSIGHIS PEAAAGGAVG LVQHGDEIEI DVENRVLRVN VDDAELARRR QEKGDAPWKP TKPRERRVSK ALKAYASMVT SADKGAVRVV ED //