Reviewed, UniProtKB/Swiss-Prot P09114 (ILVB2_TOBAC)

Names and origin

Protein names

Recommended name:
    Acetolactate synthase 2, chloroplastic
    EC=2.2.1.6
Alternative name(s):
    Acetolactate synthase II
    Acetohydroxy-acid synthase II
    ALS II

Gene names

Name:

ALS SURB

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	664 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 SuRB. 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	FAD binding Inferred from electronic annotation. Source: InterPro acetolactate synthase activity Inferred from electronic annotation. Source: EC 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 – 91	91	Chloroplast
	Chain	92 – 664	573	Acetolactate synthase 2, chloroplastic		PRO_0000035660
Regions
	Nucleotide binding	346 – 367	22	FAD By similarity
	Nucleotide binding	389 – 408	20	FAD By similarity
	Region	481 – 561	81	Thiamine pyrophosphate binding
Sites
	Metal binding	532	1	Magnesium By similarity
	Metal binding	559	1	Magnesium By similarity
	Binding site	138	1	Thiamine pyrophosphate By similarity
	Binding site	240	1	FAD By similarity
Amino acid modifications
	Disulfide bond	158 ↔ 304		By similarity
Experimental info
	Mutagenesis	191	1	P → A in S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568. Ref.1
	Mutagenesis	568	1	W → L in S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P09114-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 0CDB9EE8E6513460	FASTA	664	72,418
	10 20 30 40 50 60 MAAAAAAPSP SFSKTLSSSS SKSSTLLPRS TFPFPHHPHK TTPPPLHLTP THIHSQRRRF 70 80 90 100 110 120 TISNVISTTQ KVSETQKAET FVSRFAPDEP RKGSDVLVEA LEREGVTDVF AYPGGASMEI 130 140 150 160 170 180 HQALTRSSII RNVLPRHEQG GVFAAEGYAR ATGFPGVCIA TSGPGATNLV SGLADALLDS 190 200 210 220 230 240 VPIVAITGQV PRRMIGTDAF QETPIVEVTR SITKHNYLVM DVEDIPRVVR EAFFLARSGR 250 260 270 280 290 300 PGPVLIDVPK DIQQQLVIPD WDQPMRLPGY MSRLPKLPNE MLLEQIVRLI SESKKPVLYV 310 320 330 340 350 360 GGGCSQSSEE LRRFVELTGI PVASTLMGLG AFPTGDELSL SMLGMHGTVY ANYAVDSSDL 370 380 390 400 410 420 LLAFGVRFDD RVTGKLEAFA SRAKIVHIDI DSAEIGKNKQ PHVSICADIK LALQGLNSIL 430 440 450 460 470 480 ESKEGKLKLD FSAWRQELTV QKVKYPLNFK TFGDAIPPQY AIQVLDELTN GSAIISTGVG 490 500 510 520 530 540 QHQMWAAQYY KYRKPRQWLT SGGLGAMGFG LPAAIGAAVG RPDEVVVDID GDGSFIMNVQ 550 560 570 580 590 600 ELATIKVENL PVKIMLLNNQ HLGMVVQWED RFYKANRAHT YLGNPSNEAE IFPNMLKFAE 610 620 630 640 650 660 ACGVPAARVT HRDDLRAAIQ KMLDTPGPYL LDVIVPHQEH VLPMIPSGGA FKDVITEGDG RSSY

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-191 AND TRP-568.
[2]	Lee K.Y. Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X07645 Genomic DNA. Translation: CAA30485.1.
PIR	YCNT2. S00546.
3D structure databases
HSSP	HSSP built from PDB template 1JSC based on UniProtKB P07342.
SMR	P09114. Positions 80-661.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.2.1.6. 298.
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

ILVB2_TOBAC

Accession

Primary (citable) accession number: P09114

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)