Reviewed, UniProtKB/Swiss-Prot Q01292 (ILV5_SPIOL)

Names and origin

Protein names

Recommended name:
    Ketol-acid reductoisomerase, chloroplastic
    EC=1.1.1.86
Alternative name(s):
    Acetohydroxy-acid reductoisomerase
    Alpha-keto-beta-hydroxylacil reductoisomerase

Gene names

Name:

AHRI

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	595 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. (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. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.
Subunit structure	Tetramer of similar but non-identical chains.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the ketol-acid reductoisomerase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 72

72

Chloroplast

Chain

73 – 595

523

Ketol-acid reductoisomerase, chloroplastic

PRO_0000015631

Regions

Nucleotide binding

132 – 141

10

NADP Potential

Sites

Active site

226

1

Potential

Secondary structure

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595

Helix Strand Turn

Details...

Beta strand

91 – 93

3

Beta strand

96 – 100

5

Beta strand

103 – 109

7

Helix

112 – 117

6

Helix

118 – 121

4

Turn

122 – 124

3

Beta strand

126 – 131

6

Helix

136 – 150

15

Beta strand

156 – 161

6

Helix

168 – 173

6

Helix

178 – 180

3

Beta strand

183 – 185

3

Helix

186 – 191

6

Beta strand

194 – 198

5

Helix

202 – 215

14

Beta strand

221 – 227

7

Helix

228 – 235

8

Beta strand

244 – 253

10

Helix

255 – 265

11

Turn

266 – 269

4

Beta strand

275 – 281

7

Beta strand

283 – 285

3

Helix

287 – 297

11

Beta 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

Beta strand

586 – 588

3

Helix

590 – 592

3

Sequences

	Sequence		Length	Mass (Da)
	Q01292-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: B0EE9055097CFBA5	FASTA	595	63,754
	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

References

[1]	"Isolation, characterization and sequence analysis of a full-length cDNA clone encoding acetohydroxy acid reductoisomerase from spinach chloroplasts." Dumas R., Lebrun M., Douce R. Biochem. J. 277:469-475(1991) [PubMed: 1713446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-88. Tissue: Leaf.
[2]	"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." Biou V., Dumas R., Cohen-Addad C., Douce R., Job D., Pebay-Peyroula E. EMBO J. 16:3405-3415(1997) [PubMed: 9218783] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[3]	"Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose." Thomazeau K., Dumas R., Halgand F., Forest E., Douce R., Biou V. Acta Crystallogr. D 56:389-397(2000) [PubMed: 10739911] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 72-595.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X57073 mRNA. Translation: CAA40356.1.

PIR

S17180.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QMG	X-ray	1.60	A/B/C/D	72-595	[»]
1YVE	X-ray	1.65	I/J/K/L	72-595	[»]

ModBase

Search...

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]

Gene3D

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

PANTHER

PTHR21371. AcH_isomrdctse. 1 hit.

Pfam

PF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]

PIRSF

PIRSF000118. Ilv5_plant. 1 hit.

ProtoNet

Search...

Other Resources

LinkHub

Q01292.

Entry information

Entry name

ILV5_SPIOL

Accession

Primary (citable) accession number: Q01292

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 25, 2008
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)