ID   ILVC_BUCAP              Reviewed;         491 AA.
AC   O51888;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   16-JUN-2009, entry version 62.
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=BUsg_575;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98184963; PubMed=9516544; DOI=10.1007/PL00006760;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Sequence analysis of a 34.7-kb DNA segment from the genome of
RT   Buchnera aphidicola (endosymbiont of aphids) containing groEL, dnaA,
RT   the atp operon, gidA, and rho.";
RL   Curr. Microbiol. 36:158-163(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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.
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DR   EMBL; AF008210; AAC38126.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM68109.1; -; Genomic_DNA.
DR   RefSeq; NP_660898.1; -.
DR   HSSP; Q9HVA2; 1NP3.
DR   GeneID; 1005622; -.
DR   GenomeReviews; AE013218_GR; BUsg_575.
DR   KEGG; bas:BUsg575; -.
DR   HOGENOM; O51888; -.
DR   OMA; O51888; LKHGGIT.
DR   BioCyc; BAPH198804:BUSG575-MON; -.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH 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_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   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_0000151287.
FT   ACT_SITE    131    131       Potential.
FT   CONFLICT     36     36       N -> I (in Ref. 1; AAC38126).
SQ   SEQUENCE   491 AA;  56096 MW;  E872D203A9A219E2 CRC64;
     MNYFNKLCFR KRINEIKKCR FMKENEFKNE NKILKNKKIV IVGCGSQGLN QALNMRDSGL
     NISFALKKNS ILRKNSSWLN ATKNNFEVND YESLIPNADL VINLTPDKQH ENVVKELQKL
     MKKNSCLGYS HGFNIVECGE IIRKDITVVM VAPKCPGTEV REEFKRGFGV PTLIAVHTEN
     DPKKIGLEIA KAWAFSTGGH RAGVLESSFI AEVKSDLMGE QTILCGLLQT ASLICYEKLI
     KDKHNPSYAA KLIQYGWETI TESLKHGGIT LMMDRLSNPS KIKAFKISKK IKKILSPLFK
     KHMDDIISGS FSKEMMIDWH NNDKKLLNWR EDTKKTPFEK NILSYSEKIS EQEYYDHGTL
     MVSILKSGIE LAFETMINTG IINESAYYES LHELPLIANT IARKKLYEMN IVISDTAEYG
     SYLFSEAAYP ILKDFIMSLE KNVLGLSLPN TKIDNIELYK INEEIRNHPI EIVGKKLRKH
     MKEMKSICVA K
//