ID ILVC_CAMJE Reviewed; 340 AA. AC Q9PHN5; Q0PAN6; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 02-SEP-2026, entry version 143. 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}; OrderedLocusNames=Cj0632; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). 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; AL111168; CAL34777.1; -; Genomic_DNA. DR PIR; G81411; G81411. DR RefSeq; WP_002858483.1; NC_002163.1. DR RefSeq; YP_002344061.1; NC_002163.1. DR PDB; 7LAT; X-ray; 2.47 A; A=1-330. DR PDB; 8CY8; EM; 2.94 A; A/B/C/D/E/F/G/H/I/J/K/L=3-330. DR PDB; 8SXD; X-ray; 2.59 A; A=1-330. DR PDB; 8UPN; X-ray; 2.59 A; A=1-330. DR PDB; 8UPP; X-ray; 1.78 A; A/B/C/D/E/F/G/H/I/J/K/L=1-330. DR PDB; 8UPQ; X-ray; 2.45 A; A/B/C/D/E/F=1-340. DR AlphaFoldDB; Q9PHN5; -. DR SMR; Q9PHN5; -. DR IntAct; Q9PHN5; 41. DR STRING; 192222.Cj0632; -. DR PaxDb; 192222-Cj0632; -. DR EnsemblBacteria; CAL34777; CAL34777; Cj0632. DR GeneID; 904961; -. DR KEGG; cje:Cj0632; -. DR PATRIC; fig|192222.6.peg.624; -. DR eggNOG; COG0059; Bacteria. DR HOGENOM; CLU_033821_0_1_7; -. DR OrthoDB; 9804088at2; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000000799; 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:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.720:FF:000023; Ketol-acid reductoisomerase (NADP(+)); 1. 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 NCBIfam; NF004017; PRK05479.1; 1. DR NCBIfam; NF009940; PRK13403.1; 1. DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1. DR Pfam; PF01450; KARI_C; 1. DR Pfam; PF07991; KARI_N; 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. DR PDBsum; 7LAT; -. DR PDBsum; 8CY8; -. DR PDBsum; 8SXD; -. DR PDBsum; 8UPN; -. DR PDBsum; 8UPP; -. DR PDBsum; 8UPQ; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Magnesium; Metal-binding; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1..340 FT /note="Ketol-acid reductoisomerase (NADP(+))" FT /id="PRO_0000151297" FT DOMAIN 1..183 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197" FT DOMAIN 184..329 FT /note="KARI C-terminal knotted" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198" FT ACT_SITE 109 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 52 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 54 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 84..87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 135 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 192 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 192 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 228 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT BINDING 253 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 13..17 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 21..24 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 28..39 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 53..60 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 68..74 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 87..90 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 91..95 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 124..133 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 135..143 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 150..156 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 162..172 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:8UPP" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 185..194 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 195..200 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 202..217 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 222..226 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 232..251 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 254..267 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 270..284 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 287..297 FT /evidence="ECO:0007829|PDB:8UPP" FT TURN 298..300 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 301..311 FT /evidence="ECO:0007829|PDB:8UPP" FT HELIX 314..324 FT /evidence="ECO:0007829|PDB:8UPP" FT TURN 327..329 FT /evidence="ECO:0007829|PDB:7LAT" FT HELIX 337..340 FT /evidence="ECO:0007829|PDB:8UPQ" SQ SEQUENCE 340 AA; 36935 MW; DA556ED90C86C780 CRC64; MAITVYYDKD CDLNLIKSKK VAIIGFGSQG HAHAMNLRDN GVNVTIGLRE GSVSAVKAKN AGFEVVSVSE ASKIADVIMI LAPDEIQADI FNVEIKPNLS EGKAIAFAHG FNIHYGQIVV PKGVDVIMIA PKAPGHTVRN EFTLGGGTPC LIAIHQDESK NAKNLALSYA SAIGGGRTGI IETTFKAETE TDLFGEQAVL CGGLSALIQA GFETLVEAGY EPEMAYFECL HEMKLIVDLI YQGGIADMRY SISNTAEYGD YITGPKIITE ETKKAMKGVL KDIQNGVFAK DFILERRAGF ARMHAERKNM NDSLIEKTGR NLRAMMPWIS AKKLVDKDKN //