ID ILVC_CROS8 Reviewed; 491 AA. AC A7MQH1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 111. DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00435}; DE Short=KARI {ECO:0000255|HAMAP-Rule:MF_00435}; DE EC=1.1.1.86 {ECO:0000255|HAMAP-Rule:MF_00435}; DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000255|HAMAP-Rule:MF_00435}; DE Short=AHIR {ECO:0000255|HAMAP-Rule:MF_00435}; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435}; DE AltName: Full=Ketol-acid reductoisomerase type 2 {ECO:0000255|HAMAP-Rule:MF_00435}; DE AltName: Full=Ketol-acid reductoisomerase type II {ECO:0000255|HAMAP-Rule:MF_00435}; GN Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435}; GN OrderedLocusNames=ESA_03781; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., RA McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic RT hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). 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:0000255|HAMAP-Rule:MF_00435}. 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; Evidence={ECO:0000255|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 + 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:0000255|HAMAP-Rule:MF_00435}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00435}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00435}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP- CC Rule:MF_00435}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000255|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; CP000783; ABU78973.1; -; Genomic_DNA. DR RefSeq; WP_004387272.1; NC_009778.1. DR AlphaFoldDB; A7MQH1; -. DR SMR; A7MQH1; -. DR GeneID; 45717286; -. DR GeneID; 56732433; -. DR KEGG; esa:ESA_03781; -. DR HOGENOM; CLU_551905_0_0_6; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000000260; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 1.10.1040.10:FF:000007; Ketol-acid reductoisomerase (NADP(+)); 1. DR FunFam; 3.40.50.720:FF:000043; Ketol-acid reductoisomerase (NADP(+)); 1. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 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; IPR013328; 6PGD_dom2. DR InterPro; IPR013023; KARI. DR InterPro; IPR000506; KARI_C. DR InterPro; IPR013116; KARI_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00465; ilvC; 1. DR NCBIfam; NF003557; PRK05225.1; 1. DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1. DR Pfam; PF01450; KARI_C; 2. DR Pfam; PF07991; KARI_N; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS51851; KARI_C; 2. DR PROSITE; PS51850; KARI_N; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Magnesium; KW Metal-binding; NADP; Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1..491 FT /note="Ketol-acid reductoisomerase (NADP(+))" FT /id="PRO_1000050507" FT DOMAIN 15..208 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197" FT DOMAIN 209..344 FT /note="KARI C-terminal knotted 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198" FT DOMAIN 345..484 FT /note="KARI C-terminal knotted 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198" FT ACT_SITE 132 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 45..48 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 68 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 76 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 78 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 108..110 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 158 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 389 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 393 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" SQ SEQUENCE 491 AA; 53962 MW; 6184A8146585D3AF CRC64; MANYFNTLNL RQQLAQLGKC RFMARDEFAD GAGYLKGKKV VIVGCGAQGL NQGLNMRDSG LDVSYALRKE AIAEKRASWR KATENGFQVG TYEELIPQAD LVVNLTPDKQ HSDVVRAVQP LMKDGAALGY SHGFNIVEVG EQIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE NDPKGEGMAI AKAWAAATGG HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL VEEGTDPAYA EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKTIMAPLF QKHMDDIISG EFSSGMMADW ANDDKKLLTW REETGKTAFE NAPQYEGKIS EQEYFDKGVL MIAMVKAGVE LAFETMVAAG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG NYLFANAAVP LLKEFMTKLQ PGDLGKAVEG TAVDNAQLRD VNDAIRSHEI EKVGQKLRGY MTDMKRIAVA G //