ID ILVC_SHEAM Reviewed; 493 AA. AC A1SAS8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 02-SEP-2026, entry version 115. 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=Sama_3282; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Shewanellaceae; Shewanella. OX NCBI_TaxID=326297; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., RA Richardson P.; RT "Complete sequence of Shewanella amazonensis SB2B."; RL Submitted (DEC-2006) 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: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; CP000507; ABM01485.1; -; Genomic_DNA. DR RefSeq; WP_011761389.1; NC_008700.1. DR AlphaFoldDB; A1SAS8; -. DR SMR; A1SAS8; -. DR STRING; 326297.Sama_3282; -. DR KEGG; saz:Sama_3282; -. DR eggNOG; COG0059; Bacteria. DR HOGENOM; CLU_551905_0_0_6; -. DR OrthoDB; 9804088at2; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000009175; 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; 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..493 FT /note="Ketol-acid reductoisomerase (NADP(+))" FT /id="PRO_1000190993" FT DOMAIN 17..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..486 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 493 AA; 54431 MW; B8BFD3FFA6ED4D81 CRC64; MANYFNSLNL RQQLAQLSQC RFMDRSEFEN GCDYIKGWNI VILGCGAQGL NQGLNMRDSG LNISYALRAE AIAEKRASWK KATDNGFTVG TFEELIPQAD LVLNLTPDKQ HSNVVNTVMP LMKQGATLSY SHGFNIVEEG MQVRPDITVI MVAPKCPGTE VREEYKRGFG VPTLIAVHPE NDPRGDGLEI AKAYASATGG DRAGVLHSSF IAEVKSDLMG EQTILCGMLQ TSAILGYEKM VADGVEPGYA AKLIQQGLET ITEALKQGGI TNMMDRLSNP AKIKAFDMAE ELKGILAPLF EKHMDDIISG EFSRTMMADW ANDDANLLRW RAETNETAFE NAPSSNEHID EQTYFDKGIF LVAMIKAGVE LAFDTMVDAG IIEESAYYES LHETPLIANT IARKRLYEMN VVISDTAEYG CYLFNHAAVP LLRDYVKSMS AEYLGGGLKD SSNAVDNVRL IEVNQAIRNT AVEFIGEELR GYMKDMKRIS AAQ //