[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 73-88. TISSUE=Leaf; PubMed=1713446 [NCBI, ExPASy, EBI, Israel, Japan] Dumas R., Lebrun M., Douce R.; "Isolation, characterization and sequence analysis of a full-length cDNA clone encoding acetohydroxy acid reductoisomerase from spinach chloroplasts."; Biochem. J. 277:469-475(1991).
[2]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). DOI=10.1093/emboj/16.12.3405; PubMed=9218783 [NCBI, ExPASy, EBI, Israel, Japan] Biou V., Dumas R., Cohen-Addad C., Douce R., Job D., Pebay-Peyroula E.; "The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65-A resolution."; EMBO J. 16:3405-3415(1997).
[3]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 72-595. DOI=10.1107/S0907444900001694; PubMed=10739911 [NCBI, ExPASy, EBI, Israel, Japan] Thomazeau K., Dumas R., Halgand F., Forest E., Douce R., Biou V.; "Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose."; Acta Crystallogr. D 56:389-397(2000).

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.
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.
SUBCELLULAR LOCATION: Plastid, chloroplast.
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

Sequence databases

EMBL

X57073; CAA40356.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17180; S17180.

3D structure databases

PDB

1QMG; X-ray; 1.60 A; A/B/C/D=72-595.	[ExPASy / RCSB / EBI]
1YVE; X-ray; 1.65 A; I/J/K/L=72-595.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1QMG; -.
1YVE; -.

ModBase

Q01292.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004455;	Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009082;	Biological process: branched chain family amino acid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013023; AcH_isomrdctse.
IPR000506; AcH_isomrdctse_C.
IPR013328; DHase_multihelical.
IPR013116; IlvN.
IPR016206; KetolA_reductoisomerase_pln.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

PANTHER

PTHR21371; AcH_isomrdctse; 1.

Pfam

PF01450; IlvC; 1.
PF07991; IlvN; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000118; Ilv5_plant; 1.

Other

Q01292; -.

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

Keywords

3D-structure; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Chloroplast; Direct protein sequencing; Magnesium; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 72`	`72`	`Chloroplast.`
`CHAIN`	`73 595`	`523`	`Ketol-acid reductoisomerase, chloroplastic.`	`PRO_0000015631`
`NP_BIND`	`132 141`	`10`	`NADP (Potential).`
`ACT_SITE`	`226 226`		`Potential.`
`STRAND`	`91 93`	`3`
`STRAND`	`96 100`	`5`
`STRAND`	`103 109`	`7`
`HELIX`	`112 117`	`6`
`HELIX`	`118 121`	`4`
`TURN`	`122 124`	`3`
`STRAND`	`126 131`	`6`
`HELIX`	`136 150`	`15`
`STRAND`	`156 161`	`6`
`HELIX`	`168 173`	`6`
`HELIX`	`178 180`	`3`
`STRAND`	`183 185`	`3`
`HELIX`	`186 191`	`6`
`STRAND`	`194 198`	`5`
`HELIX`	`202 215`	`14`
`STRAND`	`221 227`	`7`
`HELIX`	`228 235`	`8`
`STRAND`	`244 253`	`10`
`HELIX`	`255 265`	`11`
`TURN`	`266 269`	`4`
`STRAND`	`275 281`	`7`
`STRAND`	`283 285`	`3`
`HELIX`	`287 297`	`11`
`STRAND`	`301 305`	`5`
`HELIX`	`308 320`	`13`
`TURN`	`321 324`	`4`
`HELIX`	`325 340`	`16`
`HELIX`	`345 350`	`6`
`HELIX`	`353 357`	`5`
`HELIX`	`359 366`	`8`
`HELIX`	`369 374`	`6`
`HELIX`	`378 408`	`31`
`HELIX`	`410 420`	`11`
`HELIX`	`440 450`	`11`
`HELIX`	`462 482`	`21`
`HELIX`	`486 493`	`8`
`HELIX`	`495 499`	`5`
`HELIX`	`502 514`	`13`
`HELIX`	`519 538`	`20`
`HELIX`	`540 545`	`6`
`HELIX`	`552 560`	`9`
`HELIX`	`563 571`	`9`
`STRAND`	`586 588`	`3`
`HELIX`	`590 592`	`3`

Sequence information

Length: 595 AA [This is the length of the unprocessed precursor]

Molecular weight: 63754 Da [This is the MW of the unprocessed precursor]

CRC64: B0EE9055097CFBA5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAATAATTFS LSSSSSTSAA ASKALKQSPK PSALNLGFLG SSSTIKACRS LKAARVLPSG 

        70         80         90        100        110        120 
ANGGGSALSA QMVSAPSINT PSATTFDFDS SVFKKEKVTL SGHDEYIVRG GRNLFPLLPD 

       130        140        150        160        170        180 
AFKGIKQIGV IGWGSQAPAQ AQNLKDSLTE AKSDVVVKIG LRKGSNSFAE ARAAGFSEEN 

       190        200        210        220        230        240 
GTLGDMWETI SGSDLVLLLI SDSAQADNYE KVFSHMKPNS ILGLSHGFLL GHLQSLGQDF 

       250        260        270        280        290        300 
PKNISVIAVC PKGMGPSVRR LYVQGKEVNG AGINSSFAVH QDVDGRATDV ALGWSIALGS 

       310        320        330        340        350        360 
PFTFATTLEQ EYKSDIFGER GILLGAVHGI VECLFRRYTE SGMSEDLAYK NTVECITGVI 

       370        380        390        400        410        420 
SKTISTKGML ALYNSLSEEG KKDFQAAYSA SYYPSMDILY ECYEDVASGS EIRSVVLAGR 

       430        440        450        460        470        480 
RFYEKEGLPA FPMGKIDQTR MWKVGEKVRS VRPAGDLGPL YPFTAGVYVA LMMAQIEILR 

       490        500        510        520        530        540 
KKGHSYSEII NESVIEAVDS LNPFMHARGV SFMVDNCSTT ARLGSRKWAP RFDYILSQQA 

       550        560        570        580        590 
LVAVDNGAPI NQDLISNFLS DPVHEAIGVC AQLRPSVDIS VTADADFVRP ELRQA

Q01292 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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