ID   ILV5_POPEU              Reviewed;          14 AA.
AC   P84534;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   22-APR-2020, entry version 44.
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-hydroxylacyl reductoisomerase;
DE   Flags: Fragment;
OS   Populus euphratica (Euphrates poplar).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=16740589; DOI=10.1093/aob/mcl106;
RA   Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA   Roepstorff P., Pais M.S.;
RT   "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL   Ann. Bot. 98:361-377(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC         acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58476; EC=1.1.1.86;
CC         Evidence={ECO:0000250|UniProtKB:Q01292};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-
CC         ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q01292};
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 from
CC       pyruvate: step 2/4.
CC   -!- SUBUNIT: Tetramer of similar but non-identical chains.
CC       {ECO:0000250|UniProtKB:Q01292}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:Q01292}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000250|UniProtKB:Q01292}.
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DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Chloroplast; Direct protein sequencing; Magnesium; NADP; Oxidoreductase;
KW   Plastid.
FT   CHAIN           <1..>14
FT                   /note="Ketol-acid reductoisomerase, chloroplastic"
FT                   /id="PRO_0000151266"
FT   NON_TER         1
FT   NON_TER         14
SQ   SEQUENCE   14 AA;  1614 MW;  58F63F7536E61967 CRC64;
     FYEKEGLPAF PMGK