Reviewed, UniProtKB/Swiss-Prot P17597 (ILVB_ARATH)

Names and origin

Protein names

Recommended name:
    Acetolactate synthase, chloroplastic
    EC=2.2.1.6
Alternative name(s):
    Acetohydroxy-acid synthase
    ALS

Gene names

Name:	CSR 1.2
Ordered Locus Names:	At3g48560
ORF Names:	T8P19.70

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	670 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	2 pyruvate = 2-acetolactate + CO2.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.
Subcellular location	Plastid › chloroplast.
Biotechnological use	Introduced by genetic manipulation and expressed in sulfonylurea resistant flax by the University of Saskatchewan.
Miscellaneous	Acetolactate synthase is the target enzyme for sulfonylurea and imidazolinone herbicides. Mutant GH 90 is resistant to imidazolinone herbicides and mutant GH 50 to sulfonylurea.
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Herbicide resistance
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
Technical term	3D-structure Complete proteome Genetically modified food
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to herbicide Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from direct assay. Source: TAIR
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acetolactate synthase activity Inferred from direct assay. Source: TAIR magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 97

97

Chloroplast

Chain

98 – 670

573

Acetolactate synthase, chloroplastic

PRO_0000035655

Regions

Nucleotide binding

352 – 373

22

FAD By similarity

Nucleotide binding

395 – 414

20

FAD By similarity

Region

487 – 567

81

Thiamine pyrophosphate binding

Sites

Metal binding

538

1

Magnesium By similarity

Metal binding

565

1

Magnesium By similarity

Binding site

144

1

Thiamine pyrophosphate By similarity

Binding site

246

1

FAD By similarity

Natural variations

Natural variant

197

1

P → S in mutant GH 50.

Natural variant

653

1

S → N in mutant GH 90.

Secondary structure

1

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670

Helix Strand Turn

Details...

Helix

99 – 108

10

Turn

109 – 111

3

Beta strand

114 – 117

4

Helix

121 – 123

3

Helix

124 – 132

9

Helix

144 – 158

15

Beta strand

162 – 166

5

Helix

170 – 173

4

Helix

176 – 185

10

Beta strand

189 – 195

7

Helix

198 – 200

3

Turn

201 – 204

4

Helix

211 – 215

5

Helix

216 – 218

3

Beta strand

219 – 224

6

Helix

228 – 230

3

Helix

231 – 243

13

Beta strand

244 – 246

3

Beta strand

249 – 255

7

Helix

256 – 260

5

Helix

274 – 279

6

Helix

286 – 298

13

Beta strand

300 – 306

7

Helix

308 – 310

3

Helix

314 – 324

11

Beta strand

328 – 330

3

Turn

332 – 336

5

Beta strand

345 – 348

4

Helix

355 – 363

9

Beta strand

365 – 371

7

Helix

376 – 379

4

Helix

382 – 384

3

Turn

385 – 388

4

Beta strand

389 – 396

8

Turn

398 – 402

5

Beta strand

403 – 405

3

Beta strand

408 – 413

6

Helix

415 – 428

14

Helix

430 – 433

4

Helix

438 – 450

13

Helix

464 – 475

12

Beta strand

480 – 483

4

Helix

487 – 494

8

Beta strand

503 – 505

3

Helix

516 – 526

11

Beta strand

532 – 537

6

Helix

538 – 543

6

Helix

544 – 546

3

Helix

547 – 553

7

Beta strand

558 – 564

7

Helix

569 – 578

10

Helix

591 – 593

3

Helix

601 – 607

7

Beta strand

612 – 615

4

Helix

618 – 630

13

Beta strand

631 – 633

3

Beta strand

635 – 640

6

Helix

657 – 659

3

Sequences

	Sequence		Length	Mass (Da)
	P17597-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: DA697A8DD155F160	FASTA	670	72,585
	10 20 30 40 50 60 MAAATTTTTT SSSISFSTKP SPSSSKSPLP ISRFSLPFSL NPNKSSSSSR RRGIKSSSPS 70 80 90 100 110 120 SISAVLNTTT NVTTTPSPTK PTKPETFISR FAPDQPRKGA DILVEALERQ GVETVFAYPG 130 140 150 160 170 180 GASMEIHQAL TRSSSIRNVL PRHEQGGVFA AEGYARSSGK PGICIATSGP GATNLVSGLA 190 200 210 220 230 240 DALLDSVPLV AITGQVPRRM IGTDAFQETP IVEVTRSITK HNYLVMDVED IPRIIEEAFF 250 260 270 280 290 300 LATSGRPGPV LVDVPKDIQQ QLAIPNWEQA MRLPGYMSRM PKPPEDSHLE QIVRLISESK 310 320 330 340 350 360 KPVLYVGGGC LNSSDELGRF VELTGIPVAS TLMGLGSYPC DDELSLHMLG MHGTVYANYA 370 380 390 400 410 420 VEHSDLLLAF GVRFDDRVTG KLEAFASRAK IVHIDIDSAE IGKNKTPHVS VCGDVKLALQ 430 440 450 460 470 480 GMNKVLENRA EELKLDFGVW RNELNVQKQK FPLSFKTFGE AIPPQYAIKV LDELTDGKAI 490 500 510 520 530 540 ISTGVGQHQM WAAQFYNYKK PRQWLSSGGL GAMGFGLPAA IGASVANPDA IVVDIDGDGS 550 560 570 580 590 600 FIMNVQELAT IRVENLPVKV LLLNNQHLGM VMQWEDRFYK ANRAHTFLGD PAQEDEIFPN 610 620 630 640 650 660 MLLFAAACGI PAARVTKKAD LREAIQTMLD TPGPYLLDVI CPHQEHVLPM IPSGGTFNDV 670 ITEGDGRIKY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a mutant acetolactate synthase gene from an imidazolinone-resistant Arabidopsis thaliana var. Columbia." Sathasivan K., Haughn G.W., Murai N. Nucleic Acids Res. 18:2188-2188(1990) [PubMed: 2336405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Molecular basis of imidazolinone herbicide resistance in Arabidopsis thaliana var Columbia." Sathasivan K., Haughn G.W., Murai N. Plant Physiol. 97:1044-1050(1991) [PubMed: 16668488] [Abstract] Cited for: VARIANT GH90. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X51514 Genomic DNA. Translation: CAA35887.1.
AL133315 Genomic DNA. Translation: CAB62345.1.
BT020540 mRNA. Translation: AAW70386.1.

IPI

IPI00522536.

PIR

YCMU. S09502.

RefSeq

NP_190425.1.

UniGene

At.22295
At.71451
At.72000

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YBH	X-ray	2.50	A	86-667	[»]
1YHY	X-ray	2.70	A	86-667	[»]
1YHZ	X-ray	2.70	A	86-667	[»]
1YI0	X-ray	2.70	A	86-667	[»]
1YI1	X-ray	2.90	A	86-667	[»]
1Z8N	X-ray	2.80	A	86-667	[»]
3E9Y	X-ray	3.00	A	87-670	[»]
3EA4	X-ray	2.80	A	87-670	[»]

ModBase

Search...

Proteomic databases

PRIDE

P17597.

Genome annotation databases

GeneID

824015.

GenomeReviews

Gene locus AT3G48560 in contig BA000014_GR.

KEGG

ath:AT3G48560.

NMPDR

fig|3702.1.peg.16095.

Organism-specific databases

TAIR

At3g48560.

Phylogenomic databases

OMA

P17597. QGLGAFD.

Enzyme and pathway databases

BRENDA

2.2.1.6. 302.

Gene expression databases

ArrayExpress

P17597.

GermOnline

AT3G48560. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR012846. Acetolactate_synth_lsu.
IPR000399. TPP_bd_CS.
IPR012001. TPP_bd_enzyme_N.
IPR011766. TPP_enzyme_bd_C.
IPR012000. TPP_enzyme_M.
[Graphical view]

Pfam

PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00118. acolac_lg. 1 hit.

PROSITE

PS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ILVB_ARATH

Accession

Primary (citable) accession number: P17597
Secondary accession number(s): Q5FV34

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)