ID   ILVC2_BACHK             Reviewed;         335 AA.
AC   Q6HKA1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-NOV-2009, entry version 33.
DE   RecName: Full=Ketol-acid reductoisomerase 2;
DE            EC=1.1.1.86;
DE   AltName: Full=Acetohydroxy-acid isomeroreductase 2;
DE   AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase 2;
GN   Name=ilvC2; OrderedLocusNames=BT9727_1693;
OS   Bacillus thuringiensis subsp. konkukian.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT59605.1; -; Genomic_DNA.
DR   RefSeq; YP_036025.1; -.
DR   GeneID; 2856800; -.
DR   GenomeReviews; AE017355_GR; BT9727_1693.
DR   KEGG; btk:BT9727_1693; -.
DR   NMPDR; fig|281309.1.peg.1665; -.
DR   HOGENOM; Q6HKA1; -.
DR   OMA; TEIQQGE; -.
DR   BioCyc; BTHU281309:BT9727_1693-MON; -.
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    335       Ketol-acid reductoisomerase 2.
FT                                /FTId=PRO_0000226160.
FT   ACT_SITE    106    106       Potential.
SQ   SEQUENCE   335 AA;  36917 MW;  8F53BEEB4FDF24E3 CRC64;
     MKTYYEQDAN VGLLQGKTVA VIGYGSQGHA QAQNLRDSGV EVVVGVRPGK SFEVAKADGF
     KVMSVSEAVR TAQVVQMLLP DEQQAHVYKA EVEENLREGQ MLLFSHGFNI HFGQINPPSY
     VDVAMVAPKS PGHLVRRVFQ EGNGVPALVA VHQDATGTAL HVALAYAKGV GCTRAGVIET
     TFQEETETDL FGEQAVLCGG VTALVKAGFE TLTEGGYRPE IAYFECLHEL KLIVDLMYEG
     GLTNMRHSIS DTAEFGDYVT GSRIVTDETK KEMKRVLTEI QQGEFAKKWI LENQAGRPTY
     NAMKKAEQNH QLEKVGEELR EMMSWIHAPK ELVKK
//