ID   ILVC_BARHE              Reviewed;         339 AA.
AC   Q6G2T6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2008, entry version 26.
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=BH10890;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27875.1; -; Genomic_DNA.
DR   RefSeq; YP_033864.1; -.
DR   GeneID; 2865556; -.
DR   GenomeReviews; BX897699_GR; BH10890.
DR   KEGG; bhe:BH10890; -.
DR   NMPDR; fig|283166.1.peg.992; -.
DR   HOGENOM; Q6G2T6; -.
DR   BioCyc; BHEN283166:BH10890-MON; -.
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    339       Ketol-acid reductoisomerase.
FT                                /FTId=PRO_0000226161.
FT   ACT_SITE    108    108       Potential.
SQ   SEQUENCE   339 AA;  37350 MW;  143769AB2CF2BFE3 CRC64;
     MRVYYDRDAN VNLIKEKKVA IVGYGSQGRA HALNLRDFGV KNVKIALRSE SATVKKAVAD
     GFEVVCVAEA AKWADLIMMA TPDELQADIY KEHIHDHLRD GAVIAFAHGL SIHFGLIEPK
     KTVDVVMIAP KGPGHTVRNE YQNGCGVPCL IAVAQDASGH AHNVALSYAC GLGGGRAGVI
     ETTFKEECET DLFGEQAVLC GGLVELIRAG YETLTEAGYA PEMAYFECLH EVKLIVDLMY
     EGGIANMNYS ISNTAEWGEY MSGPRVITDE TRAEMKRILK DIQTGKFTSN WIQEYKAGAA
     HFKGMRRLND SHPIEEVGKK LRSMMPWIKA NALVDKERN
//