ID A0A162IVD4_9HYPO Unreviewed; 401 AA. AC A0A162IVD4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 25-OCT-2017, entry version 8. 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=NOR_05031 {ECO:0000313|EMBL:OAA42182.1}; OS Metarhizium rileyi RCEF 4871. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae; OC Metarhizium. OX NCBI_TaxID=1081105 {ECO:0000313|EMBL:OAA42182.1}; RN [1] {ECO:0000313|EMBL:OAA42182.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RCEF 4871 {ECO:0000313|EMBL:OAA42182.1}; RX PubMed=27071652; DOI=10.1093/gbe/evw082; RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.; RT "Divergent and convergent evolution of fungal pathogenicity."; RL Genome Biol. Evol. 8:1374-1387(2016). 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAA42182.1}. 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; AZHC01000014; OAA42182.1; -; Genomic_DNA. DR EnsemblFungi; OAA42182; OAA42182; NOR_05031. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. 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:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1040.10; -; 3. 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; KARI. 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. 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 Isomerase {ECO:0000313|EMBL:OAA42182.1}; 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 80 245 IlvN. {ECO:0000259|Pfam:PF07991}. FT DOMAIN 253 397 IlvC. {ECO:0000259|Pfam:PF01450}. SQ SEQUENCE 401 AA; 44691 MW; 10F2AE49D8426E48 CRC64; MASRGFSKSL RAARQLATPR IQQRSYTAAR QLVRAATAAR PAVTVAQQQV RGVKTIDFAG HKEDVYERSD WPQEKLLDYF KNDTLALIGY GSQGHGQGLN LRDNGLNVIV GVRKNGKSWQ DAIQDGWVPG KNLFEVDDAI SRGTIVMNLL SDAAQSETWP AIKPQLVEGK TLYFSHGFSP VFKDLTKVDV PSNIDVILCA PKGSGRTVRS LFREGRGINS SFAVYQDVTG KAKERAIAMG VAIGSGYLYE TTFEKEVYSD LYGERGCLMG GIHGMFLAQY EVLRERGHSP SEAFNETVEE ATQSLYPLIG ANGMDWMFEA CSTTARRGAI DWTPKFKDAL KPVFNNLYDS VKDGSETQRS LDYNGQANYR EKYEAEMEEI RNLEIWRAGK AVRALRPENQ K //