ID   ILVC_BARQU              Reviewed;         339 AA.
AC   Q6FZ98;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2008, entry version 33.
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=BQ08540;
OS   Bartonella quintana (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX897700; CAF26333.1; -; Genomic_DNA.
DR   RefSeq; YP_032470.1; -.
DR   GeneID; 2866764; -.
DR   GenomeReviews; BX897700_GR; BQ08540.
DR   KEGG; bqu:BQ08540; -.
DR   NMPDR; fig|283165.1.peg.740; -.
DR   HOGENOM; Q6FZ98; -.
DR   BioCyc; BQUI283165:BQ08540-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_0000226162.
FT   ACT_SITE    108    108       Potential.
SQ   SEQUENCE   339 AA;  37325 MW;  E5BA16F0BCC8E3BD CRC64;
     MHVYYDHDAN VNLIKGKKVA IVGYGSQGHA HALNLKDSGV QDVRIALHSR SATAKKAIAD
     GFEVVRVAEA AKWADLIMMA TPDELQADIY KEHMHDDLRD GAVIAFAHGL SIHFGLIEPK
     KTVDVVMIAP KGPGHKVRNE YQRGCGVPCL IAVAQDVSGH AHDIALSYAC GIGGGRAGVM
     ETTFKEECET DLFGEQAVLC GGLVELIRAG YETLTEAGYA PEMAYFECLH EVKLIVDLLY
     EGGIANMNYS ISNTAEWGEY ISGPRVITDK TKAEMRRILK DIQTGKFTSN WIQECKAGAI
     HFKSMRRLND SHPIEEVGKK LRSMMPWIKS NALVDKKRN
//