ID ILVC_AZOSB Reviewed; 338 AA. AC A1KAB7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 16-JUN-2009, entry version 20. 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=azo3156; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=62928; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte RT Azoarcus sp. strain BH72."; RL Nat. Biotechnol. 24:1385-1391(2006). 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; AM406670; CAL95773.1; -; Genomic_DNA. DR RefSeq; YP_934659.1; -. DR SMR; A1KAB7; 1-327. DR GeneID; 4609074; -. DR GenomeReviews; AM406670_GR; azo3156. DR KEGG; azo:azo3156; -. DR OMA; A1KAB7; 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 1 338 Ketol-acid reductoisomerase. FT /FTId=PRO_1000050478. FT ACT_SITE 107 107 Potential. SQ SEQUENCE 338 AA; 36909 MW; D72BF43BDC7C4FB4 CRC64; MKVYYDKDAD LSLIKGKKVT IVGYGSQGHA HAQNLNDSGV KVTVAVRKGG ASWDKAKAAG LKVEEIAKAV KTADLVMILL PDENIPQVYK EEVEPNIKKG ATLAFAHGFN VHYNQVVPRE DLDVIMVAPK GPGHTVRSEY LRGGGVPSLI AVYQDKSGKA KDIALSYAAA NGGTKGGVIE TNFKEETETD LFGEQAVLCG GAVELVKMGF ETLTEAGYAP EMAYFECLHE LKLIVDLMYE GGIANMNYSI SNNAEYGEYV TGPEVINAQS REAMRNALKR IQTGEYAKMF IQEGKTNYPS MTARRRLNAE HPIEQVGGQL RDMMPWIKAK ALVDKSKN //