ID   ILVC_BUCML              Reviewed;         343 AA.
AC   Q9AQ96;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 40.
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;
DE   Flags: Fragment;
GN   Name=ilvC;
OS   Buchnera aphidicola subsp. Macrosiphoniella ludovicianae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wernegreen J.J., Moran N.A.;
RT   "Accelerated evolutionary rates at biosynthetic loci of Buchnera-
RT   Uroleucon.";
RL   Submitted (DEC-1999) 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; AF217557; AAK01028.1; -; Genomic_DNA.
DR   SMR; Q9AQ96; 1-343.
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; NADP;
KW   Oxidoreductase.
FT   CHAIN        <1   >343       Ketol-acid reductoisomerase.
FT                                /FTId=PRO_0000151291.
FT   ACT_SITE     65     65       Potential.
FT   NON_TER       1      1
FT   NON_TER     343    343
SQ   SEQUENCE   343 AA;  39012 MW;  67369DC0E240113C CRC64;
     RKNSILKKNQ SWINATKNNF LVGDYESLIP NADLVINLTP DKQHSNVVKE LQKLMKKDAC
     LGYSHGFNIV ENGETIRKDI TVIMVAPKCP GTEVREEYKR GFGVPTLIAV HNENDYSNMG
     LEVAKAWAFS TGGHRAGVLE SSFVAEVKSD LMGEQTILCG MLQTASLVCY EKLITTQNHP
     GYAGKLIQFG WETITESLKH GGITLMMDRL SNSSKIRAFK LSQEIKRIFS KLFQKHMDDI
     ISGDFSSKMI QDWKNKDQNL LNWRYKTKNT SFEQSPDYDK KILEQEYYDH GILMVAILKA
     GIELSFETMI QSGIMEESAY YESLHELPLI ANTIARKKLY EMN
//