ID   ILV5_YEAST              Reviewed;         395 AA.
AC   P06168;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   04-NOV-2008, entry version 88.
DE   RecName: Full=Ketol-acid reductoisomerase, mitochondrial;
DE            EC=1.1.1.86;
DE   AltName: Full=Acetohydroxy-acid reductoisomerase;
DE   AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase;
DE   Flags: Precursor;
GN   Name=ILV5; OrderedLocusNames=YLR355C; ORFNames=L9638.7;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87117524; PubMed=3027658; DOI=10.1093/nar/14.24.9631;
RA   Petersen J.G.L., Holmberg S.;
RT   "The ILV5 gene of Saccharomyces cerevisiae is highly expressed.";
RL   Nucleic Acids Res. 14:9631-9651(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 166-174.
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=95203288; PubMed=7895733; DOI=10.1002/elps.11501501210;
RA   Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA   Volpe T., Warner J.R., McLaughlin C.S.;
RT   "Protein identifications for a Saccharomyces cerevisiae protein
RT   database.";
RL   Electrophoresis 15:1466-1486(1994).
RN   [4]
RP   IDENTIFICATION OF PROBABLE N-TERMINUS.
RX   MEDLINE=97121404; PubMed=8962070; DOI=10.1073/pnas.93.25.14440;
RA   Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M.,
RA   Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.;
RT   "Linking genome and proteome by mass spectrometry: large-scale
RT   identification of yeast proteins from two dimensional gels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85; SER-317; THR-318 AND
RP   SER-355, AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
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   -!- COFACTOR: Magnesium.
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   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- MISCELLANEOUS: Present with 883000 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
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DR   EMBL; X04969; CAA28643.1; -; Genomic_DNA.
DR   EMBL; U19102; AAB67753.1; -; Genomic_DNA.
DR   PIR; A24709; A24709.
DR   RefSeq; NP_013459.1; -.
DR   HSSP; Q01292; 1QMG.
DR   DIP; DIP:6463N; -.
DR   IntAct; P06168; -.
DR   SWISS-2DPAGE; P06168; -.
DR   PeptideAtlas; P06168; -.
DR   Ensembl; YLR355C; Saccharomyces cerevisiae.
DR   GeneID; 851069; -.
DR   GenomeReviews; Y13138_GR; YLR355C.
DR   KEGG; sce:YLR355C; -.
DR   NMPDR; fig|4932.3.peg.4481; -.
DR   CYGD; YLR355c; -.
DR   SGD; S000004347; ILV5.
DR   HOGENOM; P06168; -.
DR   LinkHub; P06168; -.
DR   NextBio; 967711; -.
DR   ArrayExpress; P06168; -.
DR   GermOnline; YLR355C; Saccharomyces cerevisiae.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; TAS:SGD.
DR   GO; GO:0009082; P:branched chain family amino acid biosynthet...; TAS:SGD.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR   InterPro; IPR013023; AcH_isomrdctse.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR013328; DHase_multihelical.
DR   InterPro; IPR013116; IlvN.
DR   InterPro; IPR016207; KetolA_reductoisomerase_fun.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   PANTHER; PTHR21371; AcH_isomrdctse; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000119; Ilv5_fungal; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Direct protein sequencing; Magnesium;
KW   Mitochondrion; NADP; Oxidoreductase; Phosphoprotein; Transit peptide.
FT   TRANSIT       1     47       Mitochondrion (Potential).
FT   CHAIN        48    395       Ketol-acid reductoisomerase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000015634.
FT   NP_BIND      84     93       NADP (Potential).
FT   REGION      363    395       Hydrophilic.
FT   ACT_SITE    171    171       Potential.
FT   MOD_RES      85     85       Phosphotyrosine.
FT   MOD_RES     317    317       Phosphoserine.
FT   MOD_RES     318    318       Phosphothreonine.
FT   MOD_RES     355    355       Phosphoserine.
SQ   SEQUENCE   395 AA;  44368 MW;  D76419A6AD68E85E CRC64;
     MLRTQAARLI CNSRVITAKR TFALATRAAA YSRPAARFVK PMITTRGLKQ INFGGTVETV
     YERADWPREK LLDYFKNDTF ALIGYGSQGY GQGLNLRDNG LNVIIGVRKD GASWKAAIED
     GWVPGKNLFT VEDAIKRGSY VMNLLSDAAQ SETWPAIKPL LTKGKTLYFS HGFSPVFKDL
     THVEPPKDLD VILVAPKGSG RTVRSLFKEG RGINSSYAVW NDVTGKAHEK AQALAVAIGS
     GYVYQTTFER EVNSDLYGER GCLMGGIHGM FLAQYDVLRE NGHSPSEAFN ETVEEATQSL
     YPLIGKYGMD YMYDACSTTA RRGALDWYPI FKNALKPVFQ DLYESTKNGT ETKRSLEFNS
     QPDYREKLEK ELDTIRNMEI WKVGKEVRKL RPENQ
//