ID ILVC_BRAJA Reviewed; 339 AA. AC Q89G50; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2003, sequence version 1. DT 25-NOV-2008, entry version 38. DE RecName: Full=Ketol-acid reductoisomerase; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase; DE AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase; GN Name=ilvC; OrderedLocusNames=bll6497; OS Bradyrhizobium japonicum. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=375; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA 110; RX MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., RA Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). CC -!- CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000040; BAC51762.1; -; Genomic_DNA. DR RefSeq; NP_773137.1; -. DR HSSP; Q9HVA2; 1NP3. DR SMR; Q89G50; 1-328. DR GeneID; 1047317; -. DR GenomeReviews; BA000040_GR; bll6497. DR KEGG; bja:bll6497; -. DR NMPDR; fig|224911.1.peg.6497; -. DR HOGENOM; Q89G50; -. DR BioCyc; BJAP224911:BLL6497-MON; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009099; P:valine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00435; -; 1. DR InterPro; IPR013023; AcH_isomrdctse. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR21371; AcH_isomrdctse; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase. FT CHAIN 1 339 Ketol-acid reductoisomerase. FT /FTId=PRO_0000151283. FT ACT_SITE 108 108 Potential. SQ SEQUENCE 339 AA; 36887 MW; E221BDAEA58AF8B5 CRC64; MRVYYDRDAD LNLIKGKKVA IVGYGSQGHA HALNLKDSGV KEVAIALRKD SSSVKKAEAA GFKVMDVAEA AKWADLVMML TPDELQGDIY REHLHDNMKK GAALVFAHGL NVHFNLLDPR ADLDVLMIAP KGPGHTVRSE YQRGGGVPCL IAIAKDVSGN AHDLGLSYAS AVGGGRAGII ETTFKEECET DLFGEQVVLC GGLVELIKGG YETLVEAGYA PEMAYFECLH EVKLIVDLIY EGGIANMNYS ISNTAEYGEY VTGPRIVTAE TKAEMKRVLA DIQGGKFARD WMLENKVNQT SFKATRAKLA AHPIEEVGAK LRDMMPWIKK GALVDKSKN //