P17597 (ILVB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetolactate synthase, chloroplastic
Short name=AtALS
EC=2.2.1.6

Alternative name(s):
Acetohydroxy-acid synthase
Protein CHLORSULFURON RESISTANT 1

Gene names

Name:	ALS
Synonyms:	AHAS, CSR1, TZP5
Ordered Locus Names:	At3g48560
ORF Names:	T8P19.70

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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)

Function	Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Catalytic activity	2 pyruvate = 2-acetolactate + CO2.
Cofactor	Binds 1 magnesium ion per subunit. Ref.13 Ref.14 FAD. Ref.13 Ref.14 Binds 1 thiamine pyrophosphate per subunit. Ref.13 Ref.14
Enzyme regulation	Inhibited by asymmetric aryl disulfides, triazolopyrimidine sulfonanilide compounds, isatin derivatives, and sulfonylurea and imidazolinone herbicides. Insensitive to feed-back inhibition by branched-chain amino acids. Ref.13 Ref.16 Ref.17 Ref.18 Ref.19
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.
Subunit structure	Homodimer or homotetramer. The acetolactate synthase complex contains both large catalytic subunits and small regulatory subunits. Ref.13 Ref.21
Subcellular location	Plastid › chloroplast Probable.
Disruption phenotype	Lethal when homozygous. Ref.20
Biotechnological use	Introduced by genetic manipulation and expressed in sulfonylurea resistant plants.
Sequence similarities	Belongs to the TPP enzyme family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0-7.5. Ref.13 Ref.14

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Herbicide resistance
Cellular component	Chloroplast Plastid
Domain	Coiled coil Transit peptide
Ligand	FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
PTM	Oxidation
Technical term	3D-structure Complete proteome Genetically modified food Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to herbicide Inferred from electronic annotation. Source: UniProtKB-KW valine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast stroma Inferred from direct assay PubMed 20061580. Source: TAIR
Molecular_function	acetolactate synthase activity Inferred from direct assay PubMed 8177214. Source: TAIR flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro thiamine 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 – 55

55

Chloroplast Potential

Chain

56 – 670

615

Acetolactate synthase, chloroplastic

PRO_0000035655

Regions

Nucleotide binding

331 – 332

2

FAD

Nucleotide binding

349 – 352

4

FAD

Nucleotide binding

371 – 375

5

FAD

Nucleotide binding

395 – 396

2

FAD

Nucleotide binding

414 – 415

2

FAD

Nucleotide binding

508 – 509

2

FAD

Region

376 – 377

2

Sulfonylurea herbicides binding

Region

487 – 488

2

Thiamine pyrophosphate binding

Region

511 – 513

3

Thiamine pyrophosphate binding

Region

538 – 540

3

Thiamine pyrophosphate binding

Region

565 – 570

6

Thiamine pyrophosphate binding

Coiled coil

414 – 446

33

Potential

Sites

Metal binding

538

1

Magnesium

Metal binding

565

1

Magnesium

Metal binding

567

1

Magnesium; via carbonyl oxygen

Binding site

144

1

Thiamine pyrophosphate

Binding site

207

1

Thiamine pyrophosphate

Binding site

220

1

Imidazolinone herbicides

Binding site

246

1

FAD

Binding site

246

1

Imidazolinone herbicides; via amide nitrogen

Binding site

256

1

Sulfonylurea herbicides

Binding site

308

1

FAD; via amide nitrogen

Binding site

377

1

Imidazolinone and sulfonylurea herbicides

Binding site

574

1

Sulfonylurea herbicides

Binding site

653

1

Sulfonylurea herbicides

Amino acid modifications

Modified residue

340

1

Cysteine sulfinic acid (-SO2H)

Experimental info

Mutagenesis

122

1

A → V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. Ref.14

Mutagenesis

124

1

M → E: Reduced catalytic activity. Resistant to imidazolinone herbicides and reduced sensitivity to sulfonylurea herbicides. Ref.12

Mutagenesis

124

1

M → I: No effect on catalytic activity. Increased resistance to imidazolinone herbicides. Ref.12

Mutagenesis

197

1

P → S in csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides. Ref.9

Mutagenesis

199

1

R → A or E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. Ref.12

Mutagenesis

574

1

W → L: Increased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. Ref.14

Mutagenesis

574

1

W → S: Slightly decreased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. Ref.14

Mutagenesis

653

1

S → A: No effect on catalytic activity or sensitivity to herbicides. Ref.2 Ref.11 Ref.14 Ref.15

Mutagenesis

653

1

S → F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant. Ref.2 Ref.11 Ref.14 Ref.15

Mutagenesis

653

1

S → N in csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides. Ref.2 Ref.11 Ref.14 Ref.15

Mutagenesis

653

1

S → T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. Ref.2 Ref.11 Ref.14 Ref.15

Sequence conflict

104

1

V → A in ABJ80681. Ref.8

Sequence conflict

161

1

P → S in ABJ80681. Ref.8

Sequence conflict

208

1

E → G in ABJ80681. Ref.8

Sequence conflict

466

1

Y → H in ABJ80681. Ref.8

Sequence conflict

555

1

N → Q in AAM92569. Ref.5

Sequence conflict

560

1

V → I in AAM92569. Ref.5

Sequence conflict

575

1

E → Q in AAK68759. Ref.6

Secondary structure

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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

340 – 342

3

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

Beta strand

648 – 650

3

Helix

657 – 659

3

Sequences

	Sequence		Length	Mass (Da)
	P17597 [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]	"Isolation and characterization of plant genes coding for acetolactate synthase, the target enzyme for two classes of herbicides." Mazur B.J., Chui C.F., Smith J.K. Plant Physiol. 85:1110-1117(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-653, FUNCTION. Strain: cv. Columbia.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Saturation mutagenesis in Arabidopsis to determine frequency of herbicide resistance." Jander G., Baerson S.R., Hudak J.A., Gonzalez K.A., Gruys K.J., Last R.L. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[6]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"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.
[8]	"Cloning of Arabidopsis thaliana acetolactate synthase catalytic subunit." Jiang L., Xiang W., Wang X., Wang X., Zhang J., Xi D., Gao A. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[9]	"Transformation with a mutant Arabidopsis acetolactate synthase gene renders tobacco resistant to sulfonylurea herbicides." Haughn G.W., Smith J.K., Mazur B.J., Somerville C. Mol. Gen. Genet. 211:266-271(1988) Cited for: FUNCTION, MUTAGENESIS OF PRO-197. Strain: cv. Columbia.
[10]	"A mutation causing imidazolinone resistance maps to the csr1 locus of Arabidopsis thaliana." Haughn G.W., Somerville C.R. Plant Physiol. 92:1081-1085(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-653. Strain: cv. Columbia.
[12]	"Rational molecular design and genetic engineering of herbicide resistant crops by structure modeling and site-directed mutagenesis of acetohydroxyacid synthase." Ott K.H., Kwagh J.G., Stockton G.W., Sidorov V., Kakefuda G. J. Mol. Biol. 263:359-368(1996) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, FUNCTION, MUTAGENESIS OF MET-124 AND ARG-199.
[13]	"Expression, purification and characterization of Arabidopsis thaliana acetohydroxyacid synthase." Chang A.K., Duggleby R.G. Biochem. J. 327:161-169(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, SUBUNIT.
[14]	"Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid synthase: characterization of the catalytic properties and sensitivity to inhibitors of four defined mutants." Chang A.K., Duggleby R.G. Biochem. J. 333:765-777(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF ALA-122; TRP-574 AND SER-653.
[15]	"Effect of mutagenesis at serine 653 of Arabidopsis thaliana acetohydroxyacid synthase on the sensitivity to imidazolinone and sulfonylurea herbicides." Lee Y.T., Chang A.K., Duggleby R.G. FEBS Lett. 452:341-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-653.
[16]	"Design and synthesis of N-2,6-difluorophenyl-5-methoxyl-1,2,4-triazolo[1,5-a]-pyrimidine-2-sulfonamide as acetohydroxyacid synthase inhibitor." Chen C.N., Lv L.L., Ji F.Q., Chen Q., Xu H., Niu C.W., Xi Z., Yang G.F. Bioorg. Med. Chem. 17:3011-3017(2009) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
[17]	"Syntheses and herbicidal activity of new triazolopyrimidine-2-sulfonamides as acetohydroxyacid synthase inhibitor." Chen C.N., Chen Q., Liu Y.C., Zhu X.L., Niu C.W., Xi Z., Yang G.F. Bioorg. Med. Chem. 18:4897-4904(2010) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
[18]	"Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition, herbicidal activity, and computational studies of isatin derivatives." Wang J., Tan H., Li Y., Ma Y., Li Z., Guddat L.W. J. Agric. Food Chem. 59:9892-9900(2011) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
[19]	"Synthesis, crystal structure, in vitro acetohydroxyacid synthase inhibition, in vivo herbicidal activity, and 3D-QSAR of new asymmetric aryl disulfides." Shang J., Wang W.M., Li Y.H., Song H.B., Li Z.M., Wang J.G. J. Agric. Food Chem. 60:8286-8293(2012) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
[20]	"Comparability of imazapyr-resistant Arabidopsis created by transgenesis and mutagenesis." Schnell J., Labbe H., Kovinich N., Manabe Y., Miki B. Transgenic Res. 21:1255-1264(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[21]	"Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase." McCourt J.A., Pang S.S., King-Scott J., Guddat L.W., Duggleby R.G. Proc. Natl. Acad. Sci. U.S.A. 103:569-573(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 86-667 IN COMPLEX WITH FAD; MAGNESIUM; THIAMINE PYROPHOSPHATE AND HERBICIDES, SULFINATION AT CYS-340, SUBUNIT.
[22]	"Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase." Wang J.G., Lee P.K., Dong Y.H., Pang S.S., Duggleby R.G., Li Z.M., Guddat L.W. FEBS J. 276:1282-1290(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 87-670 IN COMPLEX WITH MAGNESIUM AND SULFONYLUREA HERBICIDES, SULFINATION AT CYS-340.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X51514 Genomic DNA. Translation: CAA35887.1.
AL133315 Genomic DNA. Translation: CAB62345.1.
CP002686 Genomic DNA. Translation: AEE78430.1.
AY124092 Genomic DNA. Translation: AAM92569.1.
AY042819 mRNA. Translation: AAK68759.1.
BT020540 mRNA. Translation: AAW70386.1.
DQ991161 mRNA. Translation: ABJ80681.1.

IPI

IPI00522536.

PIR

YCMU. S09502.

RefSeq

NP_190425.1. NM_114714.2.

UniGene

At.22295.
At.72000.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P17597.

SMR

P17597. Positions 86-667.

ModBase

Search...

Proteomic databases

PaxDb

P17597.

PRIDE

P17597.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G48560.1; AT3G48560.1; AT3G48560.

GeneID

824015.

KEGG

ath:AT3G48560.

Organism-specific databases

TAIR

At3g48560.

Phylogenomic databases

eggNOG

COG0028.

HOGENOM

HOG000258448.

InParanoid

P17597.

KO

K01652.

OMA

NNEEQGM.

PhylomeDB

P17597.

ProtClustDB

PLN02470.

Enzyme and pathway databases

UniPathway

UPA00047; UER00055.
UPA00049; UER00059.

Gene expression databases

ArrayExpress

P17597.

Genevestigator

P17597.

GermOnline

AT3G48560. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR012846. Acetolactate_synth_lsu.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]

PANTHER

PTHR18968:SF13. PTHR18968:SF13. 1 hit.

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

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Other

BindingDB

P17597.

ChEMBL

CHEMBL4263.

EvolutionaryTrace

P17597.

Entry information

Entry name

ILVB_ARATH

Accession

Primary (citable) accession number: P17597
Secondary accession number(s): A0A174 , Q5FV34, Q8L7Y7, Q94B64

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program