ID   ILVC2_BIFLO             Reviewed;         350 AA.
AC   Q8G6V1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, 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=BL0531;
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; AAN24358.1; -; Genomic_DNA.
DR   RefSeq; NP_695722.1; -.
DR   HSSP; Q9HVA2; 1NP3.
DR   GeneID; 1021989; -.
DR   GenomeReviews; AE014295_GR; BL0531.
DR   KEGG; blo:BL0531; -.
DR   HOGENOM; Q8G6V1; -.
DR   OMA; Q8G6V1; AHGFNIR.
DR   BioCyc; BLON206672:BL0531-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 2.
FT                                /FTId=PRO_0000151279.
FT   ACT_SITE    109    109       Potential.
SQ   SEQUENCE   350 AA;  38552 MW;  E91A4B60022CA63E CRC64;
     MAATIWYEKD ADLSVFDGKK VAILGYGSQG HAHALNLRDS GVDVVVGLRP TSKSVEFAKE
     QGLEVKPVGE AVAEADVVMI LLPDQYQAAV YKKDVEPNLK PGAALAFAHG FNIHYGYIKP
     SEDHPVFMVA PKGPGHIVRR EYAAGRGVPV VVAVEQDPDG KTWPLCLAYA KALGALRAGA
     IKTTFTEETE TDLFGEQDVL MGGINHLCDL GFDVLTEAGY QPEIAYFEVF HELKMLVDLA
     NEGGLNKARW SCSDTAQYGD YTSTVITEET KKRMQYQLKR IQDGSFAKEF MDDQAAGAPK
     FKKLQEEYSH PHLETVGPKL RAMFSWNNAE AKDKDETESF NGKIARTQVQ
//