ID ILVC_STRS2 Reviewed; 340 AA. AC A4W3V8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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 1 {ECO:0000255|HAMAP-Rule:MF_00435}; DE AltName: Full=Ketol-acid reductoisomerase type I {ECO:0000255|HAMAP-Rule:MF_00435}; GN Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435}; GN OrderedLocusNames=SSU98_1889; OS Streptococcus suis (strain 98HAH33). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=391296; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=98HAH33; RX PubMed=17375201; DOI=10.1371/journal.pone.0000315; RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., RA Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., RA Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., RA Yang R., Wang J., Yu J.; RT "A glimpse of streptococcal toxic shock syndrome from comparative genomics RT of S. suis 2 Chinese isolates."; RL PLoS ONE 2:E315-E315(2007). 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 + 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: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 + 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: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; CP000408; ABP93047.1; -; Genomic_DNA. DR AlphaFoldDB; A4W3V8; -. DR SMR; A4W3V8; -. DR KEGG; ssv:SSU98_1889; -. DR HOGENOM; CLU_033821_0_1_9; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. 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; 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; Branched-chain amino acid biosynthesis; Magnesium; KW Metal-binding; NADP; Oxidoreductase. FT CHAIN 1..340 FT /note="Ketol-acid reductoisomerase (NADP(+))" FT /id="PRO_1000050579" FT DOMAIN 1..182 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197" FT DOMAIN 183..328 FT /note="KARI C-terminal knotted" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198" FT ACT_SITE 108 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 26..29 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 49 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 53 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 83..86 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 134 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 195 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 227 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 252 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" SQ SEQUENCE 340 AA; 37356 MW; 6BC139BF65F109C6 CRC64; MTVTMQYEKD VTVAALDGKR IAVIGYGSQG HAHAQNLRDT GHDVIIGVRA GKSFDKAKED GFETFEVAEA AKQADVIMIL APDEIQADLY NEEIAPNLEA GNALGFAHGF NVHFEFIKVP ADVDVFMCAP KGPGHLVRRT FEEGFGVPAL YAVYQDATGN AKHIAMDWAK GVGSARVGLL ETTFKEETEE DLFGEQAVLC GGLTALMQAG FEVLTEAGYA PELAYFEVLH EMKLIVDLVY EGGFKKMRQS ISNTAEFGDY VSGPRVITDQ VKENMKAVLA DIQSGKFAND FVNDYKAGRP RMEAYRKEAE NLEIEKVGAE LRKAMPFVGR NDDDAFKIYN //