ID ILV5_PEA Reviewed; 581 AA. AC O82043; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 55. DE RecName: Full=Ketol-acid reductoisomerase, chloroplastic; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid reductoisomerase; DE AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase; DE Flags: Precursor; GN Name=PGAAIR; OS Pisum sativum (Garden pea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. G2; RA Gu X., Xu Y., Wu J., Hou X., Chen Z., Zhu Y.; RL Submitted (AUG-1998) 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 -!- COFACTOR: Magnesium (By similarity). 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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; Y17796; CAA76854.1; -; mRNA. DR PIR; T06825; T06825. DR HSSP; Q01292; 1QMG. DR SMR; O82043; 69-578. DR BRENDA; 1.1.1.86; 287. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0009082; P:branched chain family amino acid biosynthet...; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013023; AcH_isomrdctse. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR013116; IlvN. DR InterPro; IPR016206; KetolA_reductoisomerase_pln. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR PANTHER; PTHR21371; AcH_isomrdctse; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR PIRSF; PIRSF000118; Ilv5_plant; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Chloroplast; Magnesium; NADP; Oxidoreductase; Plastid; KW Transit peptide. FT TRANSIT 1 58 Chloroplast (By similarity). FT CHAIN 59 581 Ketol-acid reductoisomerase, FT chloroplastic. FT /FTId=PRO_0000015630. FT ACT_SITE 210 210 Potential. SQ SEQUENCE 581 AA; 62852 MW; D6F2B8DF4B2AC697 CRC64; MAAVTSSCST AISASSKTLA KPVAASFAPT NLSFSKLSPQ SIRARRSITV GSALGATKVS APPATHPVSL DFETSVFKKE RVNLAGHEEY IVRGGRDLFH LLPDAFKGIK QIGVIGWGSQ GPAQAQNLRD SLVEAKSDIV VKVGLRKGSS SFNEAREAGF SEEKGTLGDI WETISGSDLV LLLISDSAQA DNYEKIFSHL KPNSILGLSH GFLLGHLQSI GLDFPKNFSV IAVCPKGMGP SVRRLYVQGK EINGAGINSS FGVHQDVDGR ATNVALGWSV ALGSPFTFAT TLEQEYKSDI FGERGILLGA VHGIVESLFR RYTENGMSED LAYKNTVESI TGVISKTIST QGMLAVYNAL SEDGKKEFEK AYSASFYPCM EILYECYEDV ASGSEIRSVV LAGRRFYEKE GLPAFPMGKI DQTRMWKVGE RVRSTRPAGD LGPLYPFTAG VFVAMMMAQI EVLRKKGHSY SEIINESVIE SVDSLNPFMH ARGVSFMVDN CSTTARLGSR KWAPRFDYIL TQQALVAVDS GAPINQDLIS NFVSDPVHGA IQVCAELRPT LDISVPAAAD FVRPELRQCS N //