P09342 (ILVB1_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetolactate synthase 1, chloroplastic
EC=2.2.1.6

Alternative name(s):
ALS I
Acetohydroxy-acid synthase I
Acetolactate synthase I

Gene names

Name:

ALS SURA

Organism

Nicotiana tabacum (Common tobacco)

Taxonomic identifier

4097 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana

Protein attributes

Sequence length	667 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.
Miscellaneous	There are two distinct ALS genes in tobacco. The enzyme shown here is derived from the ALS gene on locus SuRA. Acetolactate synthase is the target enzyme for sulfonylurea and imidazolinone herbicides.
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
PTM	Disulfide bond
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 electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetolactate synthase activity Inferred from electronic annotation. Source: EC 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 – 94	94	Chloroplast
	Chain	95 – 667	573	Acetolactate synthase 1, chloroplastic		PRO_0000035659
Regions
	Nucleotide binding	349 – 370	22	FAD By similarity
	Nucleotide binding	392 – 411	20	FAD By similarity
	Region	484 – 564	81	Thiamine pyrophosphate binding
Sites
	Metal binding	535	1	Magnesium By similarity
	Metal binding	562	1	Magnesium By similarity
	Binding site	141	1	Thiamine pyrophosphate By similarity
	Binding site	243	1	FAD By similarity
Amino acid modifications
	Disulfide bond	161 ↔ 307		Ref.3
Experimental info
	Mutagenesis	194	1	P → Q in C3; highly resistant to sulfonylurea herbicides. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P09342 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: DF2674EC6CA827C2	FASTA	667	72,868
	10 20 30 40 50 60 MAAAAPSPSS SAFSKTLSPS SSTSSTLLPR STFPFPHHPH KTTPPPLHLT HTHIHIHSQR 70 80 90 100 110 120 RRFTISNVIS TNQKVSQTEK TETFVSRFAP DEPRKGSDVL VEALEREGVT DVFAYPGGAS 130 140 150 160 170 180 MEIHQALTRS SIIRNVLPRH EQGGVFAAEG YARATGFPGV CIATSGPGAT NLVSGLADAL 190 200 210 220 230 240 LDSVPIVAIT GQVPRRMIGT DAFQETPIVE VTRSITKHNY LVMDVEDIPR VVREAFFLAR 250 260 270 280 290 300 SGRPGPILID VPKDIQQQLV IPDWDQPMRL PGYMSRLPKL PNEMLLEQIV RLISESKKPV 310 320 330 340 350 360 LYVGGGCSQS SEDLRRFVEL TGIPVASTLM GLGAFPTGDE LSLSMLGMHG TVYANYAVDS 370 380 390 400 410 420 SDLLLAFGVR FDDRVTGKLE AFASRAKIVH IDIDSAEIGK NKQPHVSICA DIKLALQGLN 430 440 450 460 470 480 SILESKEGKL KLDFSAWRQE LTEQKVKHPL NFKTFGDAIP PQYAIQVLDE LTNGNAIIST 490 500 510 520 530 540 GVGQHQMWAA QYYKYRKPRQ WLTSGGLGAM GFGLPAAIGA AVGRPDEVVV DIDGDGSFIM 550 560 570 580 590 600 NVQELATIKV ENLPVKIMLL NNQHLGMVVQ WEDRFYKANR AHTYLGNPSN EAEIFPNMLK 610 620 630 640 650 660 FAEACGVPAA RVTHRDDLRA AIQKMLDTPG PYLLDVIVPH QEHVLPMIPS GGAFKDVITE GDGRSSY

References

[1]	"The molecular basis of sulfonylurea herbicide resistance in tobacco." Lee K.Y., Townsend J., Tepperman J., Black M., Chui C.-F., Mazur B., Dunsmuir P., Bedbrook J. EMBO J. 7:1241-1248(1988) [PubMed: 16453837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF PRO-194.
[2]	Lee K.Y. Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Structural and functional role of cysteinyl residues in tobacco acetolactate synthase." Shin H.J., Chong C.K., Chang S.I., Choi J.D. Biochem. Biophys. Res. Commun. 271:801-806(2000) [PubMed: 10814542] [Abstract] Cited for: DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07644 Genomic DNA. Translation: CAA30484.1.
PIR	YCNT1. S00545.
3D structure databases
ProteinModelPortal	P09342.
SMR	P09342. Positions 83-664.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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	Search...

Entry information

Entry name

ILVB1_TOBAC

Accession

Primary (citable) accession number: P09342

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	October 19, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program