ID A0A0D2DC68_9EURO Unreviewed; 404 AA. AC A0A0D2DC68; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 17-FEB-2016, entry version 7. DE RecName: Full=Ketol-acid reductoisomerase, mitochondrial {ECO:0000256|PIRNR:PIRNR000119}; DE EC=1.1.1.86 {ECO:0000256|PIRNR:PIRNR000119}; DE AltName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000256|PIRNR:PIRNR000119}; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|PIRNR:PIRNR000119}; GN ORFNames=Z517_11990 {ECO:0000313|EMBL:KIW75216.1}; OS Fonsecaea pedrosoi CBS 271.37. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; OC Fonsecaea. OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW75216.1}; RN [1] {ECO:0000313|EMBL:KIW75216.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW75216.1}; RG The Broad Institute Genomics Platform; RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M., RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC {ECO:0000256|PIRNR:PIRNR000119}. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC {ECO:0000256|PIRNR:PIRNR000119}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR000119}; CC Note=Binds 2 magnesium ions per subunit. CC {ECO:0000256|PIRNR:PIRNR000119}; CC -!- SUBCELLULAR LOCATION: Mitochondrion CC {ECO:0000256|PIRNR:PIRNR000119}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|PIRNR:PIRNR000119}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KN846976; KIW75216.1; -; Genomic_DNA. DR RefSeq; XP_013279024.1; XM_013423570.1. DR EnsemblFungi; KIW75216; KIW75216; Z517_11990. DR GeneID; 25311480; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-UniRule. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1040.10; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR013023; Ketol-acid_reductoisomrdctse. DR InterPro; IPR016207; KetolA_reductoisomerase_fun. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR PIRSF; PIRSF000119; Ilv5_fungal; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000119}; KW Branched-chain amino acid biosynthesis KW {ECO:0000256|PIRNR:PIRNR000119}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000119}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000119}; KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000119}; KW NADP {ECO:0000256|PIRNR:PIRNR000119}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000119}. FT DOMAIN 84 249 IlvN. {ECO:0000259|Pfam:PF07991}. FT DOMAIN 257 401 IlvC. {ECO:0000259|Pfam:PF01450}. SQ SEQUENCE 404 AA; 44954 MW; 66F130534E3C0D4C CRC64; MASKNFARTL RTASKQKISA PAVQRRSIAT ALATRPVVAA AQRPAFAAPA QQQKRGVKTI DFAGTKETVF EREDWPREKL LDYFKNDTLA LIGYGSQGHG QGLNLRDNGL NVIIGVRKNG ASWKEAEQDG WIPGKNLFEV DEAIDRGTII MNLLSDAAQS ETWPAIKPKL TKGKTLYFSH GFSPVFKDLT KVDVPKDIDV ILVAPKGSGR TVRSLFREGR GINSSVAVYQ DVTGKAEEKA IALGVAIGSG YLYKTTFEKE VYSDLYGERG CLMGGIHGMF LAQYEVLRER GHSPSEAFNE TVEEATQSLY PLIGANGMDW MYAACSTTAR RGAIDWSSKF KDTLKPLFNQ LYDSVRDGTE TKRSLEFNSA PDYREKYEKE MQDIRDLEIW RAGKAVRSLR PENQ //