ID ILVC1_BACHK Reviewed; 336 AA. AC Q6HLF4; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 04-NOV-2008, entry version 29. DE RecName: Full=Ketol-acid reductoisomerase 1; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase 1; DE AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase 1; GN Name=ilvC1; OrderedLocusNames=BT9727_1283; OS Bacillus thuringiensis subsp. konkukian. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=180856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). 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; AE017355; AAT62183.1; -; Genomic_DNA. DR RefSeq; YP_035617.1; -. DR GeneID; 2858689; -. DR GenomeReviews; AE017355_GR; BT9727_1283. DR KEGG; btk:BT9727_1283; -. DR NMPDR; fig|281309.1.peg.1257; -. DR HOGENOM; Q6HLF4; -. DR BioCyc; BTHU281309:BT9727_1283-MON; -. 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 1 336 Ketol-acid reductoisomerase 1. FT /FTId=PRO_0000226159. FT ACT_SITE 107 107 Potential. SQ SEQUENCE 336 AA; 36779 MW; 4049B6C0159A71D5 CRC64; MAKVYYEKDV TVNVLKEKKV AIIGYGSQGH AHAQNLRDNG FDVVVGLRKG KSWDKAKEDG FSVYTVAEAA KKADVVMILL PDELQPEVYE AEIAPNLQAG NSLVFAHGFN VHFDQVKPPV NVDVFLVAPK GPGHLVRRTF VEGGAVPALF AVYQDATGVA TEKALSYADG IGATRAGVLE TTFKEETETD LFGEQAVLCG GVTALVKAGF ETLVDAGYQP ELAYFECLHE LKLIVDLMYE GGLENMRYSV SDTAQWGDFV SGPRVVTEDT KKAMDTVLAE IQDGTFARGW IAEHKAGRPN FHATNEKENE HEIEVVGRKL REMMPFVQPR VKAGVK //