ID ILVC_AQUAE Reviewed; 333 AA. AC O67289; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-JUN-2009, entry version 60. 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=aq_1245; OS Aquifex aeolicus. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=63363; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex RT aeolicus."; RL Nature 392:353-358(1998). 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; AE000657; AAC07240.1; -; Genomic_DNA. DR PIR; F70407; F70407. DR RefSeq; NP_213853.1; -. DR HSSP; Q9HVA2; 1NP3. DR GeneID; 1192727; -. DR GenomeReviews; AE000657_GR; aq_1245. DR KEGG; aae:aq_1245; -. DR NMPDR; fig|224324.1.peg.868; -. DR HOGENOM; O67289; -. DR OMA; O67289; AHGFNIR. DR BioCyc; AAEO224324:AQ_1245-MON; -. DR BRENDA; 1.1.1.86; 189781. 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_dom. 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 1 333 Ketol-acid reductoisomerase. FT /FTId=PRO_0000151269. FT ACT_SITE 108 108 Potential. SQ SEQUENCE 333 AA; 37307 MW; 8E55F82619698B55 CRC64; MAKIYYDEDA SLDILKDKVI AILGYGSQGH AHALNLRDSG LNVIIGLHEG SRSREKAKAD GFEVYTPREA AKRADIIMFL IPDTVQPEVY KNEVEPELNS SKTLAFAHGF NIHFRQIVPP KDVDVFMVAP KGPGHLVRWM YTEGKGVPAL VAIHQDASGT CKDKALAYAK GIGATRAGVI ETTFKEETET DLFGEQMVLC GGVTALIKAG FETLVNAGYQ PEVAYFECLH ELKLIVDLIY EHGISGMRYS ISDTAKYGDV TRGERIYKVV KPVMEKTLEE IQKGEFAREW ILENKAGRPV YYALLERDRE HLVEKVGEEL RKMMPWLGKK ELK //