ID ILVD1_METAC Reviewed; 553 AA. AC Q8TPV2; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 04-NOV-2026, entry version 120. DE RecName: Full=Dihydroxy-acid dehydratase 1 {ECO:0000255|HAMAP-Rule:MF_00012}; DE Short=DAD 1 {ECO:0000255|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012}; GN Name=ilvD1 {ECO:0000255|HAMAP-Rule:MF_00012}; GN OrderedLocusNames=MA_1802; OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / OS C2A). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=188937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A; RX PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., RA Zinder S.H., Lander E., Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and RT physiological diversity."; RL Genome Res. 12:532-542(2002). 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; AE010299; AAM05208.1; -; Genomic_DNA. DR RefSeq; WP_011021805.1; NC_003552.1. DR AlphaFoldDB; Q8TPV2; -. DR SMR; Q8TPV2; -. DR FunCoup; Q8TPV2; 176. DR STRING; 188937.MA_1802; -. DR EnsemblBacteria; AAM05208; AAM05208; MA_1802. DR GeneID; 1473691; -. DR KEGG; mac:MA_1802; -. DR HOGENOM; CLU_014271_4_2_2; -. DR InParanoid; Q8TPV2; -. DR OMA; AADDHYS; -. DR OrthoDB; 8674at2157; -. DR PhylomeDB; Q8TPV2; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000002487; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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:0016836; F:hydro-lyase activity; IBA:GO_Central. 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; NF002068; PRK00911.1; 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..553 FT /note="Dihydroxy-acid dehydratase 1" FT /id="PRO_0000103539" FT ACT_SITE 470 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 78 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 119 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 120 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 121 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 191 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT BINDING 444 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" FT MOD_RES 121 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012" SQ SEQUENCE 553 AA; 58668 MW; 182C355FAD48C3D1 CRC64; MRSAIIKEGP ERAANRSLLK ATGVTDSEMK KPFIAVVNSW NEIVPGHIHL DKLAEAVKAG IRNAGGVPFE FHTIGVCDGL AMGHEGMKYS LPSREVIEDT IELMVRAHQF DGMVLIPTCD KIVPGHLMAA GRLDIPAIVV TGGPMLPGYV DDKYTDLISV FEGVGAYSAG KLSEAELKRL ENLSCAGAGS CAGMFTANTM ACMTEALGLS LPGCATAHAV DAKKVRIAKE SGERIVALVK ENLTPRKIVT QKSFENAIMV DMAVGGSTNT TLHLPALAHE FGLELPLKTF DELSRTTPHL ISLRPGGPNF MLHFDRAGGV EAVVQRLASK LHLDQLTVNG KTIGENLDEL EIVNPKLNAE IITTLENPIH AEGGIAVLKG SLAPDGSVVK QAAVDPKMRV HTGPAKVYDC EEDAMKSILA GDVKPGDIVV IRYEGPKGGP GMREMLAATA AIGGMGLLES VALITDGRFS GGTRGPCIGH VSPEASEGGP IGLVKDGDLI EINIPERILN LKVTEEELEK RKAAFVPPKK EVTGYLARYQ RSVHSANTGG IVD //