ID A0A162IVD4_METRR Unreviewed; 401 AA. AC A0A162IVD4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 27-NOV-2024, entry version 32. 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 (strain RCEF 4871) (Nomuraea rileyi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium. OX NCBI_TaxID=1081105 {ECO:0000313|EMBL:OAA42182.1, ECO:0000313|Proteomes:UP000243498}; RN [1] {ECO:0000313|EMBL:OAA42182.1, ECO:0000313|Proteomes:UP000243498} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCEF 4871 {ECO:0000313|EMBL:OAA42182.1, RC ECO:0000313|Proteomes:UP000243498}; 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: CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2- CC acetolactate + NADPH + H(+); 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 + NADPH + H(+); 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|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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A162IVD4; -. DR STRING; 1081105.A0A162IVD4; -. DR OMA; RAMFSWL; -. DR OrthoDB; 1090117at2759; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000243498; Unassembled WGS sequence. 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 FunFam; 1.10.1040.10:FF:000003; Ketol-acid reductoisomerase, mitochondrial; 1. DR FunFam; 1.10.1040.10:FF:000005; Ketol-acid reductoisomerase, mitochondrial; 1. DR FunFam; 1.10.1040.10:FF:000013; Ketol-acid reductoisomerase, mitochondrial; 1. DR FunFam; 3.40.50.720:FF:000167; Ketol-acid reductoisomerase, mitochondrial; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR00465; ilvC; 1. DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR PIRSF; PIRSF000119; Ilv5_fungal; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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:OAA42182.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000119}; 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|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000119}; KW Reference proteome {ECO:0000313|Proteomes:UP000243498}. FT DOMAIN 61..251 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000259|PROSITE:PS51850" FT DOMAIN 252..399 FT /note="KARI C-terminal knotted" FT /evidence="ECO:0000259|PROSITE:PS51851" FT BINDING 260 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 260 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 264 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 296 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 300 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198" 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 //