[1]	PROTEIN SEQUENCE. TISSUE=Leaf; DOI=10.1093/aob/mcl106; PubMed=16740589 [NCBI, ExPASy, EBI, Israel, Japan] Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S., Roepstorff P., Pais M.S.; "Proteome profiling of Populus euphratica Oliv. upon heat stress."; Ann. Bot. 98:361-377(2006).

Comments

CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP⁺ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP⁺ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
COFACTOR: Magnesium (By similarity).
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4 .
PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4 .
SUBUNIT: Tetramer of similar but non-identical chains (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
SIMILARITY: Belongs to the ketol-acid reductoisomerase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

ModBase

P84534.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0004455;	Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from EC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013023; AcH_isomrdctse.
Graphical view of domain structure.

PANTHER

PTHR21371; AcH_isomrdctse; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Chloroplast; Direct protein sequencing; Magnesium; NADP; Oxidoreductase; Plastid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >14`	`>14`	`Ketol-acid reductoisomerase, chloroplastic.`	`PRO_0000151266`
`NON_TER`	`1 1`
`NON_TER`	`14 14`

Sequence information

Length: 14 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 1614 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 58F63F7536E61967 [This is a checksum on the sequence]

        10 
FYEKEGLPAF PMGK

P84534 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools