ID   ILV5_NEUCR              Reviewed;         402 AA.
AC   P38674; Q7RVD5; Q8X0I9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   16-JUN-2009, entry version 75.
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=ilv-2; ORFNames=B11H24.150, NCU03608;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93013010; PubMed=1398116; DOI=10.1016/0378-1119(92)90018-K;
RA   Sista H., Bowman B.;
RT   "Characterization of the ilv-2 gene from Neurospora crassa encoding
RT   alpha-keto-beta-hydroxylacyl reductoisomerase.";
RL   Gene 120:115-118(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22542210; PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
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DR   EMBL; M84189; AAB00797.1; -; Genomic_DNA.
DR   EMBL; AL670005; CAD21284.1; -; Genomic_DNA.
DR   EMBL; AABX02000011; EAA32099.1; -; Genomic_DNA.
DR   PIR; JC1428; JC1428.
DR   RefSeq; XP_961335.1; -.
DR   HSSP; Q9HVA2; 1NP3.
DR   GeneID; 3877517; -.
DR   KEGG; ncr:NCU03608; -.
DR   NMPDR; fig|5141.1.peg.843; -.
DR   BioCyc; NCRA-XX3-01:NCRA-XX3-01-007356-MON; -.
DR   BRENDA; 1.1.1.86; 266.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched chain family amino acid biosynthet...; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013023; AcH_isomrdctse.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR013116; IlvN.
DR   InterPro; IPR016207; KetolA_reductoisomerase_fun.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Mitochondrion; NADP; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1     26       Mitochondrion (Potential).
FT   CHAIN        27    402       Ketol-acid reductoisomerase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000015632.
FT   NP_BIND      90     99       NADP (Potential).
FT   ACT_SITE    177    177       Potential.
FT   CONFLICT    358    358       T -> R (in Ref. 1; AAB00797).
FT   CONFLICT    392    393       Missing (in Ref. 1; AAB00797).
SQ   SEQUENCE   402 AA;  44623 MW;  246F795898D2A174 CRC64;
     MAARNCTKAL RPLARQLATP AVQRRTFVAA ASAVRASVAV KAVAAPARQQ VRGVKTMDFA
     GHKEEVHERA DWPAEKLLDY FKNDTLALIG YGSQGHGQGL NLRDNGLNVI VGVRKNGKSW
     EDAIQDGWVP GKNLFDVDEA ISRGTIVMNL LSDAAQSETW PHIKPQITKG KTLYFSHGFS
     PVFKDLTKVE VPTDVDVILV APKGSGRTVR SLFREGRGIN SSFAVYQDVT GKAKEKAVAL
     GVAVGSGYLY ETTFEKEVYS DLYGERGCLM GGIHGMFLAQ YEVLRERGHS PSEAFNETVE
     EATQSLYPLI GAHGMDWMFD ACSTTARRGA IDWTPKFKDA LKPVFNNLYD SVKNGDETKR
     SLEYNSQPDY RERYEAELDE IRNLEIWRAG KAVRSLRPEN QK
//