ID A0A1S2MZW7_9MICC Unreviewed; 613 AA. AC A0A1S2MZW7; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 24-JUL-2024, entry version 27. DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490, ECO:0000256|HAMAP-Rule:MF_00012}; DE Short=DAD {ECO:0000256|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490, ECO:0000256|HAMAP-Rule:MF_00012}; GN Name=ilvD {ECO:0000256|HAMAP-Rule:MF_00012}; GN ORFNames=BK826_06145 {ECO:0000313|EMBL:OIJ35919.1}; OS Rothia kristinae. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Rothia. OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OIJ35919.1, ECO:0000313|Proteomes:UP000179540}; RN [1] {ECO:0000313|EMBL:OIJ35919.1, ECO:0000313|Proteomes:UP000179540} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCT-H5 {ECO:0000313|EMBL:OIJ35919.1, RC ECO:0000313|Proteomes:UP000179540}; RA Huang B.; RT "Draft genome sequence of strain LCT isolated from the Shenzhou X RT spacecraft of China."; RL Submitted (OCT-2016) 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00029304}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810; CC Evidence={ECO:0000256|ARBA:ARBA00029304}; 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:0000256|HAMAP-Rule:MF_00012}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00012}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00012}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis CC acid cofactor. {ECO:0000256|HAMAP-Rule:MF_00012}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 3/4. CC {ECO:0000256|ARBA:ARBA00029437, ECO:0000256|HAMAP-Rule:MF_00012}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 3/4. {ECO:0000256|ARBA:ARBA00029436, ECO:0000256|HAMAP- CC Rule:MF_00012}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00012}. CC -!- SIMILARITY: Belongs to the IlvD/Edd family. CC {ECO:0000256|ARBA:ARBA00006486, ECO:0000256|HAMAP-Rule:MF_00012}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00012}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OIJ35919.1}. 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; MODZ01000006; OIJ35919.1; -; Genomic_DNA. DR RefSeq; WP_075514841.1; NZ_MODZ01000006.1. DR AlphaFoldDB; A0A1S2MZW7; -. DR OrthoDB; 9807077at2; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000179540; Unassembled WGS sequence. 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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule. 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; IPR000581; DiOHA_6PGluconate_deHydtase. DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS. DR InterPro; IPR037237; IlvD/EDD_N. DR NCBIfam; TIGR00110; ilvD; 1. DR PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1. DR PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-RELATED; 1. DR Pfam; PF00920; ILVD_EDD; 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 {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_00012}; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00012}; KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304, KW ECO:0000256|HAMAP-Rule:MF_00012}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00012}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00012}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00012}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00012}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00012}. FT REGION 567..588 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 519 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012" FT BINDING 81 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012" FT BINDING 123 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00012" FT BINDING 493 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012" FT MOD_RES 124 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012" SQ SEQUENCE 613 AA; 65863 MW; 34466D064A2805D3 CRC64; MPALRSRTST HGRNMAGARA LWRATGMKKE DFGKPIVAIA NSFTQFVPGH VHLKNMGALV ASAVEEAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSRDVI ADSVEYMVNA HRADALVCIS NCDKITPGML MAAMRLNIPV VFVSGGPMES GAPVEGVLEH RIDLVDAMAY AVDEQVSDAQ LAQIEENACP TCGSCSGMFT ANSMNCLTEA LGLSLPGNGT TLATQIARKE LFLKAGRTVV ELAKRYYEQD DESVLPRNVA TKASFRNAMS LDVAMGGSTN TVLHILAAAQ EAEVDFTLKD IDEISRHVPC LCKVAPNSTQ FHIEHVHRAG GIPAILGELD RAGLLEHDGV HTVHADSVDA WLDEWDIRRD TASERARELY LAAPGGVRTT QAFSTANRFE SHDTDAEFGC IRSVEHAYTK DGGLAVLYGN IAEDGAVIKT AGIDEYLFRF IGKAFVVESQ DEAVFEILSK HVQPGDIVVI QYEGPKGGPG MQEMLYPTSY LKGLGLGKEC ALITDGRFSG GTSGISIGHI SPEAASGGAV GLIRTGDEIE IDVTQRLLQV NVSDEELARR REERGPLPWK PTKPRERQVS KALRAYASMV TSADKGAVRV VPE //