ID ILVC_ALHEH Reviewed; 338 AA. AC Q0AB89; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 25-NOV-2008, entry version 23. 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=Mlg_0544; OS Alkalilimnicola ehrlichei (strain MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000453; ABI55898.1; -; Genomic_DNA. DR RefSeq; YP_741388.1; -. DR GeneID; 4270299; -. DR GenomeReviews; CP000453_GR; Mlg_0544. DR KEGG; aeh:Mlg_0544; -. DR NMPDR; fig|187272.6.peg.517; -. DR HOGENOM; Q0AB89; -. 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 1 338 Ketol-acid reductoisomerase. FT /FTId=PRO_1000050476. FT ACT_SITE 107 107 Potential. SQ SEQUENCE 338 AA; 36223 MW; 53B2C7AF5EC008DA CRC64; MQVYYDKDAD LSIIQGKKVA VIGYGSQGHA HANNLKESGV DVVVGLREGS SSAAKAQKAG LAVASIEDAA AQADVVMILA PDEHQAVIYH NQIAPNVKPG AAIAFAHGFN IHFGQIQPAA DLDVIMVAPK GPGHLVRSTY VEGGGVPSLI AIHQDATGKA KDIALSYASA NGGGRAGVIE TSFREETETD LFGEQAVLCG GITSLIQAGF ETLVEAGYAP EMAYFECLHE TKLIVDLLYQ GGIANMRYSI SNTAEYGDFT RGPRVINEES REAMREILAE IQEGEFAREF VLENQAGCPT LTARRRLAAE HEIEVVGERL RGMMPWINAN KLVDKDKN //