ID ILVC_PROM1 Reviewed; 331 AA. AC A2C482; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 05-OCT-2016, entry version 68. 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=NATL1_17361; OS Prochlorococcus marinus (strain NATL1A). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167555; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL1A; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino CC acids (BCAA). Catalyzes an alkyl-migration followed by a ketol- CC acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3- CC dihydroxy-isovalerate. In the isomerase reaction, S2AL is CC rearranged via a Mg-dependent methyl migration to produce 3- CC hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, CC this 2-ketoacid undergoes a metal-dependent reduction by NADPH to CC yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000255|HAMAP- CC Rule:MF_00435}. CC -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC {ECO:0000255|HAMAP-Rule:MF_00435}. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC {ECO:0000255|HAMAP-Rule:MF_00435}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-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 CC from 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 -!- SIMILARITY: Contains 1 IlvC domain. {ECO:0000255|HAMAP- CC Rule:MF_00435}. CC -!- SIMILARITY: Contains 1 IlvN domain. {ECO:0000255|HAMAP- CC 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; CP000553; ABM76292.1; -; Genomic_DNA. DR RefSeq; WP_011824291.1; NC_008819.1. DR ProteinModelPortal; A2C482; -. DR STRING; 167555.NATL1_17361; -. DR EnsemblBacteria; ABM76292; ABM76292; NATL1_17361. DR KEGG; pme:NATL1_17361; -. DR PATRIC; 23021105; VBIProMar31285_1769. DR eggNOG; ENOG4105C6M; Bacteria. DR eggNOG; COG0059; LUCA. DR HOGENOM; HOG000016230; -. DR KO; K00053; -. DR OMA; FETCHEL; -. DR OrthoDB; POG091H063Y; -. DR BioCyc; PMAR167555:GI3K-1773-MONOMER; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000002592; Chromosome. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1040.10; -; 1. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR013023; Ketol-acid_reductoisomrdctse. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Magnesium; Metal-binding; NADP; Nucleotide-binding; KW Oxidoreductase. FT CHAIN 1 331 Ketol-acid reductoisomerase (NADP(+)). FT /FTId=PRO_1000050554. FT DOMAIN 15 178 IlvN. {ECO:0000255|HAMAP-Rule:MF_00435}. FT DOMAIN 184 327 IlvC. {ECO:0000255|HAMAP-Rule:MF_00435}. FT NP_BIND 25 28 NADP. {ECO:0000255|HAMAP-Rule:MF_00435}. FT NP_BIND 83 86 NADP. {ECO:0000255|HAMAP-Rule:MF_00435}. FT ACT_SITE 108 108 {ECO:0000255|HAMAP-Rule:MF_00435}. FT METAL 191 191 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00435}. FT METAL 191 191 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00435}. FT METAL 195 195 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00435}. FT METAL 227 227 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00435}. FT METAL 231 231 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00435}. FT BINDING 51 51 NADP. {ECO:0000255|HAMAP-Rule:MF_00435}. FT BINDING 53 53 NADP. {ECO:0000255|HAMAP-Rule:MF_00435}. FT BINDING 134 134 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00435}. FT BINDING 252 252 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00435}. SQ SEQUENCE 331 AA; 36262 MW; E620EF4B1395C3DD CRC64; MAKLFYDSDA DLGLLQDKTV AIIGYGSQGH AHALNLKDSG IKVVVGLYEG SRSASKAKSD GLEVLSVAEA SERADWIMIL LPDEFQKDVY SKEIAPHLKA GKILSFAHGF NIRFELIKPP EFVDVVMIAP KGPGHTVRWE YQNGQGVPAL FAIEQDASGN ARALAMAYAK GIGGTRAGIL ETNFKEETET DLFGEQAVLC GGLSELVKAG FETLVEAGYQ PELAYFECLH EVKLIVDLMV KGGLTAMRDS ISNTAEYGDY VSGPRLITKE TKEEMKNILA DIQDGTFAKN FVKECDAGKP EMKRIRQKDS ELPIEKVGKT LRSMFSWLKS D //