ID   ILVC2_BACCR             Reviewed;         335 AA.
AC   Q81F27;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 37.
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=BC_1779;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22608415; PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(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.
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DR   EMBL; AE016877; AAP08753.1; -; Genomic_DNA.
DR   RefSeq; NP_831552.1; -.
DR   HSSP; Q9HVA2; 1NP3.
DR   GeneID; 1204128; -.
DR   GenomeReviews; AE016877_GR; BC_1779.
DR   KEGG; bce:BC1779; -.
DR   HOGENOM; Q81F27; -.
DR   BioCyc; BCER226900:BC_1779-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.
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_0000151275.
FT   ACT_SITE    106    106       Potential.
SQ   SEQUENCE   335 AA;  36921 MW;  07741D1B931B3E9F CRC64;
     MKTYYEKDAN VELLQGKTVA VVGYGSQGHA QAQNLRDSGV EVVVGVRPGK SYEVAKADGF
     EVMSVSEAVR TAQVVQMLLP DEQQAHVYKA EVEENLREGQ MLLFSHGFNI HFGQINPPSY
     VDVAMVAPKS PGHLVRRVFQ EGNGVPALVA VHQDATGTAL HVALAYAKGV GCTRAGVIET
     TFQEETETDL FGEQAVLCGG VTALVKAGFE TLTEGGYRPE IAYFECLHEL KLIVDLMYEG
     GLTTMRHSIS DTAEFGDYVT GSRIVTDETK KEMKRVLTEI QQGEFAKKWI LENQAGRPTY
     NAMKKAEQNH QLEKVGAELR EMMSWIHAPK ELVKK
//