ID A0A0D2DC68_9EURO Unreviewed; 404 AA. AC A0A0D2DC68; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 03-JUL-2019, entry version 21. 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, ECO:0000313|Proteomes:UP000053029}; RN [1] {ECO:0000313|EMBL:KIW75216.1, ECO:0000313|Proteomes:UP000053029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW75216.1, RC ECO:0000313|Proteomes:UP000053029}; 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: CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2- CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; CC Evidence={ECO:0000256|PIRNR:PIRNR000119}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)- CC 2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; CC Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, CC ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.86; Evidence={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, ECO:0000256|PROSITE- CC ProRule:PRU01198}. 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 EuPathDB; FungiDB:Z517_11990; -. DR OrthoDB; 720924at2759; -. DR Proteomes; UP000053029; Unassembled WGS sequence. DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi. DR GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule. 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:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1040.10; -; 3. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR013023; KARI. DR InterPro; IPR000506; KARI_C. DR InterPro; IPR013116; KARI_N. DR InterPro; IPR016207; KetolA_reductoisomerase_fun. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. 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. DR PROSITE; PS51851; KARI_C; 1. DR PROSITE; PS51850; KARI_N; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000119, KW ECO:0000256|PROSITE-ProRule:PRU01198}; KW Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR000119, KW ECO:0000256|PROSITE-ProRule:PRU01198}; KW Complete proteome {ECO:0000313|Proteomes:UP000053029}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE- KW ProRule:PRU01198}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE- KW ProRule:PRU01198}; Mitochondrion {ECO:0000256|PIRNR:PIRNR000119}; KW NADP {ECO:0000256|PIRNR:PIRNR000119}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE- KW ProRule:PRU01198}; KW Reference proteome {ECO:0000313|Proteomes:UP000053029}. FT DOMAIN 65 255 KARI N-terminal Rossmann. FT {ECO:0000259|PROSITE:PS51850}. FT DOMAIN 256 403 KARI C-terminal knotted. FT {ECO:0000259|PROSITE:PS51851}. FT METAL 264 264 Magnesium 1. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 264 264 Magnesium 2. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 268 268 Magnesium 1. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 300 300 Magnesium 2. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 304 304 Magnesium 2. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT BINDING 326 326 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU01198}. 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 //