ID A6UW80_META3 Unreviewed; 329 AA. AC A6UW80; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435}; DE Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435}; DE EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435}; DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435}; DE Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435}; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435}; GN Name=ilvC {ECO:0000256|HAMAP-Rule:MF_00435}; GN OrderedLocusNames=Maeo_1175 {ECO:0000313|EMBL:ABR56752.1}; OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / OS Nankai-3). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=419665 {ECO:0000313|EMBL:ABR56752.1, ECO:0000313|Proteomes:UP000001106}; RN [1] {ECO:0000313|EMBL:ABR56752.1, ECO:0000313|Proteomes:UP000001106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3 RC {ECO:0000313|Proteomes:UP000001106}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus aeolicus Nankai-3."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids CC (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction CC of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In CC the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl CC migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the CC reductase reaction, this 2-ketoacid undergoes a metal-dependent CC reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. CC {ECO:0000256|HAMAP-Rule:MF_00435}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00435}; 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|HAMAP-Rule:MF_00435}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00435}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00435}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC {ECO:0000256|ARBA:ARBA00004885, ECO:0000256|HAMAP-Rule:MF_00435}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864, ECO:0000256|HAMAP- CC Rule:MF_00435}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|HAMAP-Rule:MF_00435, CC ECO:0000256|PROSITE-ProRule:PRU01198}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}. 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; CP000743; ABR56752.1; -; Genomic_DNA. DR RefSeq; WP_011973884.1; NC_009635.1. DR AlphaFoldDB; A6UW80; -. DR STRING; 419665.Maeo_1175; -. DR GeneID; 75304626; -. DR KEGG; mae:Maeo_1175; -. DR eggNOG; arCOG04465; Archaea. DR HOGENOM; CLU_033821_0_1_2; -. DR OrthoDB; 6064at2157; -. DR BRENDA; 1.1.1.86; 3261. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000001106; Chromosome. 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 6.10.240.10; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013023; KARI. DR InterPro; IPR000506; KARI_C. DR InterPro; IPR013116; KARI_N. DR InterPro; IPR014359; KARI_prok. 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; PIRSF000116; IlvC_gammaproteo; 2. 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00435}; KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304, KW ECO:0000256|HAMAP-Rule:MF_00435}; Isomerase {ECO:0000313|EMBL:ABR56752.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00435}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00435}; NADP {ECO:0000256|HAMAP-Rule:MF_00435}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00435}. FT DOMAIN 1..181 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000259|PROSITE:PS51850" FT DOMAIN 182..327 FT /note="KARI C-terminal knotted" FT /evidence="ECO:0000259|PROSITE:PS51851" FT ACT_SITE 107 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 24..27 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 47 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 52 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 133 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 190 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 190 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 226 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 230 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 251 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" SQ SEQUENCE 329 AA; 36348 MW; 8D72B89581B32026 CRC64; MKVYYEEDAN YDAVKDKTIA VIGYGSQGMA QSCNMKDSGL NVIVGLRPNG ASWEKAKADG HTVMSVEEAA EKADIIHILI PDEVQKDVYN NQIKQHLTEG KTLSFSHGYN VHFKYIDPIK GVNVIMVAPK SPGAMVRRTY TEGFGVPGLV CVERDETGDA LDIALGMAKA EGLTKAGVIK TTFKEETETD LFGEQAVLCG GVTELIKAGF DTLVEAGYSP EMAYFETCNE LKLIVDLIYQ KGLAGMWNDV SNTAEYGGFV TRERVINEES RKAMREILKE IQNGKFARDW ALENVSGIPH LNAMRRLEDE SLLETTGKKL RKMCGLQKD //