ID C5YN64_SORBI Unreviewed; 591 AA. AC C5YN64; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 02-SEP-2026, entry version 88. DE RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490}; DE EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490}; GN ORFNames=SORBI_3007G167800 {ECO:0000313|EMBL:EES15173.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EES15173.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EES15173.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). RN [2] {ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=29161754; DOI=10.1111/tpj.13781; RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D., RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A., RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.; RT "The Sorghum bicolor reference genome: improved assembly, gene annotations, RT a transcriptome atlas, and signatures of genome organization."; RL Plant J. 93:338-354(2018). 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|ARBA:ARBA00052865}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695; CC Evidence={ECO:0000256|ARBA:ARBA00052865}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|ARBA:ARBA00034078}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 3/4. CC {ECO:0000256|ARBA:ARBA00029437}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 3/4. {ECO:0000256|ARBA:ARBA00029436}. CC -!- SIMILARITY: Belongs to the IlvD/Edd family. CC {ECO:0000256|ARBA:ARBA00006486}. 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; CM000766; EES15173.1; -; Genomic_DNA. DR AlphaFoldDB; C5YN64; -. DR SMR; C5YN64; -. DR FunCoup; C5YN64; 912. DR STRING; 4558.C5YN64; -. DR Gramene; EES15173; EES15173; SORBI_3007G167800. DR KEGG; sbi:8057977; -. DR eggNOG; KOG2448; Eukaryota. DR HOGENOM; CLU_014271_4_1_1; -. DR InParanoid; C5YN64; -. DR OMA; STQGRNM; -. DR OrthoDB; 3851628at2759; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000000768; Chromosome 7. DR ExpressionAtlas; C5YN64; baseline and differential. DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IBA:GO_Central. DR GO; GO:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniPathway. DR FunFam; 3.50.30.80:FF:000005; Dihydroxy-acid dehydratase chloroplastic; 1. DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1. DR HAMAP; MF_00012; IlvD; 1. DR InterPro; IPR050165; DHAD_IlvD/Edd. 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; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 1. DR PANTHER; PTHR21000:SF5; DIHYDROXY-ACID DEHYDRATASE, MITOCHONDRIAL; 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 {ECO:0000256|ARBA:ARBA00022714}; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605}; KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. FT DOMAIN 68..385 FT /note="Dihydroxy-acid/6-phosphogluconate dehydratase N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00920" FT DOMAIN 397..587 FT /note="Dihydroxy-acid/6-phosphogluconate dehydratase C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF24877" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..10 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 591 AA; 63181 MW; 145DD23264B06E33 CRC64; MQSMALTSPS LPAAGPVTGR RLQRVRATAV SDEPKLNKYS ARITEPKSQG ASQAVLYGVG LTDADLRKPQ VGVSSVWYEG NTCNMHLLRL AEAVRDGVRE AGMVGFRFNT VGVSDAISMG TRGMCYSLQS RDLIADSIET VMGAQHYDAN ISIPGCDKNM PGTIMAMGRL NRPSIMIYGG TIKPGHFQGN SYDIVSAFQC YGEYVSGSIT DEQRKNVLRN SCPGAGACGG MYTANTMASA IETLGMSLPY SSSTPAEDPL KLEECHLAGK YLLELLKMDL KPKDIITEKS LRNAMVIVMA LGGSTNAVLH LIAIARSVGL HLTLDDFQKV SDQVPFLADL KPSGKYVMED LHKIGGTPAV IHYLLEQGLL DGDCMTVTGK TLAENAKIFP PLSEGQQIIR PLDNPIKSTG HIQILYGNLA PEGSVAKITG KEGLFFSGPA LVFEGEESMI TAISENPANF KGKVVVIRGE GPKGGPGMPE MLTPTSAIMG AGLGKECALL TDGRFSGGSH GFVVGHICPE AQEGGPIGLV QSGDVITIDV SKRVIDVDLT EQQLEERRRK WTPPPYKSTR GALWKYIKLV APASRGCVTD E //