ID   ILVC_BUCBP              Reviewed;         491 AA.
AC   Q89A20;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, 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;
GN   Name=ilvC; OrderedLocusNames=bbp_541;
OS   Buchnera aphidicola subsp. Baizongia pistaciae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=135842;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27240.1; -; Genomic_DNA.
DR   RefSeq; NP_778135.1; -.
DR   HSSP; Q9HVA2; 1NP3.
DR   GeneID; 1058333; -.
DR   GenomeReviews; AE016826_GR; bbp_541.
DR   KEGG; bab:bbp541; -.
DR   HOGENOM; Q89A20; -.
DR   BioCyc; BAPH224915:BBP_541-MON; -.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; IPR014359; KetolA_reductoisomerase_bac.
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   PIRSF; PIRSF000116; IlvC_gammaproteo; 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    491       Ketol-acid reductoisomerase.
FT                                /FTId=PRO_0000151288.
FT   ACT_SITE    133    133       Potential.
SQ   SEQUENCE   491 AA;  55968 MW;  9583C462A6D0EA82 CRC64;
     MGSNYFNSLN FRQKLIQLRQ CTLIRKEEFS ETFKILKGKN IVIVGCGSQG LNQGLNMRDS
     GLNVKYALRK NSIISQRSSW KRAIDNKFLV GTCEELIPTA DLVINLTPDK QHEHVVDVLQ
     NLMKKNSILG FSHGFNIIEF GQKIRQDITV IMVAPKCPGT EVREEYKRNF GVPTLISVHL
     DNDCHNIGLE VAKEWATAIG GHRAGVLHSS FSAEVKSDLM GEQTILCGLL QTGSVLCYDK
     LISQGHDCHY AVKLVQSGWE VITESLKHGG ITLMFDRLSN TAKIRAYKLS NDLKKILSPI
     FKKHMDDILS GYYSKNMMLD WKNDDKQLKI WRRSIQNTSF EQCSISHITL LEHEYFENGL
     LMVAIIRAGV ELAFEIMIEA GIKEESAYYE SLHELPLIAN TIARKRLYEM NLIISDTAEY
     GSHLFFQSAF PLLQDFMNTL EHGDLGNKML DQAINNVDLN YINTTIRNHP VEHIGQKLRR
     YMTNIKQINC Y
//