ID A0A6G6TCB0_9GAMM Unreviewed; 616 AA. AC A0A6G6TCB0; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 14-DEC-2022, entry version 9. DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000256|HAMAP-Rule:MF_00012}; DE Short=DAD {ECO:0000256|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000256|HAMAP-Rule:MF_00012}; GN Name=ilvD {ECO:0000256|HAMAP-Rule:MF_00012, GN ECO:0000313|EMBL:QIG04056.1}; GN ORFNames=GTK47_01240 {ECO:0000313|EMBL:QIG04056.1}; OS Proteus sp. ZN5. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=2697019 {ECO:0000313|EMBL:QIG04056.1, ECO:0000313|Proteomes:UP000501562}; RN [1] {ECO:0000313|EMBL:QIG04056.1, ECO:0000313|Proteomes:UP000501562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZN5 {ECO:0000313|EMBL:QIG04056.1, RC ECO:0000313|Proteomes:UP000501562}; RA Peng K.; RT "The genomic epidemiology of tigecycline resistance gene tet(X) variants in RT a swine farm in China."; RL Submitted (JAN-2020) 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 --------------------------------------------------------------------------- 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; CP047639; QIG04056.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6G6TCB0; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000501562; Chromosome. 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; -; 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 Pfam; PF00920; ILVD_EDD; 1. DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1. DR TIGRFAMs; TIGR00110; ilvD; 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 565..584 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 517 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 491 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 616 AA; 65706 MW; 97FF5F9F61DA9EF9 CRC64; MPKYRSATTT HGRNMAGARA LWRATGMTDA DFGKPIIAVV NSFTQFVPGH VHLRDLGKLV AEQIEAAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI ADSVEYMVNA HCADAMVCIS NCDKITPGML MASLRLNIPV IFVSGGPMEA GKTKLSDQLI KLDLVDAMIQ GANPNVSDAD SEQIERSACP TCGSCSGMFT ANSMNCLTEA LGLSQPGNGS LLATHADRET LFINAGKRIV ELTKRYYEKD DESALPRNIA KKEAFENAMI LDIAMGGSTN TVLHLLAAAQ EGEVDFTMED IDRLSRQVPH LCKVAPSTQK YHMEDVHRAG GVMGILGELD RAGLLNRNVD NILGLTLPET LAQYDVMLTQ DEQVKSMFQA GPAGIRTTKA FSQNCRWPTL DTDRENGCIR SKEHAYSQDG GLAVLSGNLA VDGCIVKTAG VDEDNLIFSG PAKVYESQDD AVEAILGGKV VAGDVVIIRY EGPKGGPGMQ EMLYPTSYLK SMGLGKACAL ITDGRFSGGT SGLSIGHVSP EAANGGVIGL VEEGDIVSIN IPTREISLKV DDKTLSARRD AQNSRGDKAW TPQNRQRQVS FALRAYASLA TSADKGAVRD KSKLGG //