ID ILVC_ARTS2 Reviewed; 341 AA. AC A0JXZ6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Ketol-acid reductoisomerase; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase; DE AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase; GN Name=ilvC; OrderedLocusNames=Arth_2537; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290399; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., RA Nakatsu C.H., Richardson P.; RT "Complete sequence of chromosome 1 of Arthrobacter sp. FB24."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000454; ABK03916.1; -; Genomic_DNA. DR RefSeq; YP_832016.1; -. DR GeneID; 4444945; -. DR GenomeReviews; CP000454_GR; Arth_2537. DR KEGG; art:Arth_2537; -. DR TIGR; Arth_2537; -. DR OMA; A0JXZ6; AHGFNIR. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009099; P:valine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00435; -; 1. DR InterPro; IPR013023; AcH_isomrdctse. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR21371; AcH_isomrdctse; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase. FT CHAIN 1 341 Ketol-acid reductoisomerase. FT /FTId=PRO_1000050477. FT ACT_SITE 108 108 Potential. SQ SEQUENCE 341 AA; 37189 MW; 3FE814BF4EFAAC1E CRC64; MTEMFYDDDA DLSIIQGRKV AIVGYGSQGH AHALNLRDSG VEVTIALKEG SSSIAKAQDA GFTVKNVADA AEWADVIMIL APDQHQRSIY NDSIKDKLTP GKALAFAHGF NIRFGYIKAP EGVDVILIAP KAPGHTVRRE FEAGRGIPDI IAVEQDATGA AWDLAKSYAK AIGGTRAGVI KTTFTEETET DLFGEQAVLC GGVSQLVQYG FETLTEAGYQ PQIAYFEVLH ELKLIVDLMW EGGIAKQRWS VSDTAEYGDY VSGPRVITPE VKENMKAVLA DIQNGAFAKR FIEDQDNGGV EFKALRAKAE QHPIESVGRE LRGLFSWQQQ DEDYVEGSAA R //