ID   ILVC1_BIFLO             Reviewed;         350 AA.
AC   Q8G6V2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Ketol-acid reductoisomerase 1;
DE            EC=1.1.1.86;
DE   AltName: Full=Acetohydroxy-acid isomeroreductase 1;
DE   AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase 1;
GN   Name=ilvC1; OrderedLocusNames=BL0530;
OS   Bifidobacterium longum.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=216816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN24357.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_695721.1; -.
DR   HSSP; Q9HVA2; 1NP3.
DR   GeneID; 1023093; -.
DR   GenomeReviews; AE014295_GR; BL0530.
DR   KEGG; blo:BL0530; -.
DR   HOGENOM; Q8G6V2; -.
DR   BioCyc; BLON206672:BL0530-MON; -.
DR   BRENDA; 1.1.1.86; 39917.
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    350       Ketol-acid reductoisomerase 1.
FT                                /FTId=PRO_0000151278.
FT   ACT_SITE    109    109       Potential.
SQ   SEQUENCE   350 AA;  38560 MW;  FD3E3B700BF65247 CRC64;
     MAAQIWYEND GDLSVLEGKK VAIIGYGSQG HAHALNLRDS GVDVVVGLRP TSKSVDFAKE
     QGLEVKSVAE ASAEADVIMI LAPDQYQRTI WANDIEPNIK PGAAVAFAHG FNIHYGYIKP
     SEDHPVFMVA PKGPGHIVRR EYAAGRGVPV VVAVEQDPRG DGWALTLAYA KALGALRAGA
     IKTTFKEETE TDLFGEQNVL MGGVNKLVEM GFEVLTDAGY QPEIAYFEVC HELKMLVDLM
     NEGGLNKARW SCSDTAQYGD YVNTVINEDC RKRMEYHLQR IQDGSFAKEF IDDQDAGAPH
     FKELQEKYSN ERIETVGPKL RAMFSWNKDG VKDADEANSF TGKIARAQVQ
//