ID A0A0D2DC68_9EURO Unreviewed; 404 AA. AC A0A0D2DC68; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 19-JAN-2022, entry version 29. 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; 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., Nusbaum C., RA 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, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC 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)-2- CC ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; CC Evidence={ECO:0000256|ARBA:ARBA00000850, 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 -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC {ECO:0000256|ARBA:ARBA00004885}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR000119}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PIRNR:PIRNR000119, CC ECO:0000256|PROSITE-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 STRING; 1442368.A0A0D2DC68; -. DR EnsemblFungi; KIW75216; KIW75216; Z517_11990. DR GeneID; 25311480; -. DR VEuPathDB; FungiDB:Z517_11990; -. DR HOGENOM; CLU_033821_1_2_1; -. DR OrthoDB; 720924at2759; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. 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|ARBA:ARBA00022605, KW ECO:0000256|PIRNR:PIRNR000119}; KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304, KW ECO:0000256|PIRNR:PIRNR000119}; Isomerase {ECO:0000313|EMBL:KIW75216.1}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE- KW ProRule:PRU01198}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR000119}; KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000119}; KW NADP {ECO:0000256|PIRNR:PIRNR000119}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE- KW ProRule:PRU01198}; Reference proteome {ECO:0000313|Proteomes:UP000053029}. FT DOMAIN 65..255 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000259|PROSITE:PS51850" FT DOMAIN 256..403 FT /note="KARI C-terminal knotted" FT /evidence="ECO:0000259|PROSITE:PS51851" FT METAL 264 FT /note="Magnesium 1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 264 FT /note="Magnesium 2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 268 FT /note="Magnesium 1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 300 FT /note="Magnesium 2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 304 FT /note="Magnesium 2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 326 FT /note="Substrate" FT /evidence="ECO:0000256|PROSITE-ProRule: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 //