ID   ILVC_ACICJ              Reviewed;         339 AA.
AC   A5G1L8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 13.
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=Acry_2559;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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.
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DR   EMBL; CP000697; ABQ31750.1; -; Genomic_DNA.
DR   RefSeq; YP_001235669.1; -.
DR   GeneID; 5160054; -.
DR   GenomeReviews; CP000697_GR; Acry_2559.
DR   KEGG; acr:Acry_2559; -.
DR   OMA; A5G1L8; AHGFNIR.
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   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    339       Ketol-acid reductoisomerase.
FT                                /FTId=PRO_1000050471.
FT   ACT_SITE    108    108       Potential.
SQ   SEQUENCE   339 AA;  36747 MW;  115C767E96D37D42 CRC64;
     MRVYYDSDAD VNLIKAKKVA VVGYGSQGHA HALNLKESGV KELVVALRKG SAAVAKAEAA
     GLRVMTPEEA AAWADVVMIL TPDEGQGDLY RDSLAANLKP GAAIAFAHGL NIHFNLIEPR
     ADIDVFMIAP KGPGHTVRSE YQRGGGVPCL VAVAQNPSGN ALDIALSYAS AIGGGRAGII
     ETTFKEECET DLFGEQTVLC GGLVELIKAG FETLVEAGYA PEMAYFECLH EVKLIVDLIY
     EGGIANMNYS ISNTAEYGEY VTGPRMITPE TKAEMKRVLD DIQKGRFTRD WMLENKVNQT
     NFKAMRRANA AHPIEEVGEK LRAMMPWIKK GALVDKTRN
//