ID ILVC1_STRCO Reviewed; 332 AA. AC Q9Z565; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 25-NOV-2008, entry version 58. DE RecName: Full=Ketol-acid reductoisomerase 1; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase 1; DE AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase 1; GN Name=ilvC1; Synonyms=ilvC; OrderedLocusNames=SCO5514; GN ORFNames=SC8D9.26; OS Streptomyces coelicolor. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1902; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX MEDLINE=21996410; PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., RA Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces RT coelicolor A3(2)."; RL Nature 417:141-147(2002). 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; AL939124; CAB37590.1; -; Genomic_DNA. DR PIR; T35830; T35830. DR RefSeq; NP_629649.1; -. DR HSSP; Q9HVA2; 1NP3. DR GeneID; 1100954; -. DR GenomeReviews; AL645882_GR; SCO5514. DR KEGG; sco:SCO5514; -. DR NMPDR; fig|100226.1.peg.5466; -. DR HOGENOM; Q9Z565; -. DR BioCyc; SCOE100226:SCO5514-MON; -. 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. 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 1 332 Ketol-acid reductoisomerase 1. FT /FTId=PRO_0000151363. FT ACT_SITE 108 108 Potential. SQ SEQUENCE 332 AA; 36254 MW; 84D0A2E698B3504E CRC64; MAELFYDADA DLSIIQGRKV AVIGYGSQGH AHALSLRDSG VDVRVGLHEG SKSKAKAEEQ GLRVVPVAEA AAEADVIMIL VPDPIQAEVY EKDIKDNLKD GDALFFGHGL NIRYGFIKPP AGVDVCMVAP KGPGHLVRRQ YEEGRGVPCI AAVEQDATGN AFALALSYAK GIGGTRAGVI KTTFTEETET DLFGEQAVLC GGTAALVKAG FETLTEAGYQ PEIAYFECLH ELKLIVDLMY EGGLEKMRWS ISETAEWGDY VTGPRIITDA TKAEMKKVLA EIQDGTFAKN WMDEYHGGLK KYNEYKKQDS EHLLETTGKE LRKLMSWVDE EA //