Reviewed, UniProtKB/Swiss-Prot P27818 (ILVB1_BRANA)

Names and origin

Protein names	Recommended name:     Acetolactate synthase 1, chloroplastic     EC=2.2.1.6 Alternative name(s):     Acetolactate synthase I     Acetohydroxy-acid synthase I     ALS I
Organism	Brassica napus (Rape)
Taxonomic identifier	3708 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Brassica

Protein attributes

Sequence length	655 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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	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
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 – 82	82	Chloroplast By similarity
	Chain	83 – 655	573	Acetolactate synthase 1, chloroplastic		PRO_0000035656
Regions
	Nucleotide binding	337 – 358	22	FAD By similarity
	Nucleotide binding	380 – 399	20	FAD By similarity
	Region	472 – 552	81	Thiamine pyrophosphate binding
Sites
	Metal binding	523	1	Magnesium By similarity
	Metal binding	550	1	Magnesium By similarity
	Binding site	129	1	Thiamine pyrophosphate By similarity
	Binding site	231	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27818-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 1BEAD7D7A0DAD91A	FASTA	655	71,289
	10 20 30 40 50 60 MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKDSS RLHRPLAISA VLNSPVNVAP 70 80 90 100 110 120 PSPEKTDKNK TFVSRYAPDE PRKGADILVE ALERQGVETV FAYPGGASME IHQALTRSST 130 140 150 160 170 180 IRNVLPRHEQ GGVFAAEGYA RSSGKPGICI ATSGPGATNL VSGLADAMLD SVPLVAITGQ 190 200 210 220 230 240 VPRRMIGTDA FQETPIVEVT RSITKHNYLV MDVDDIPRIV QEAFFLATSG RPGPVLVDVP 250 260 270 280 290 300 KDIQQQLAIP NWDQPMRLPG YMSRLPQPPE VSQLGQIVRL ISESKRPVLY VGGGSLNSSE 310 320 330 340 350 360 ELGRFVELTG IPVASTLMGL GSYPCNDELS LQMLGMHGTV YANYAVEHSD LLLAFGVRFD 370 380 390 400 410 420 DRVTGKLEAF ASRAKIVHID IDSAEIGKNK TPHVSVCGDV KLALQGMNKV LENRAEELKL 430 440 450 460 470 480 DFGVWRSELS EQKQKFPLSF KTFGEAIPPQ YAIQILDELT EGKAIISTGV GQHQMWAAQF 490 500 510 520 530 540 YKYRKPRQWL SSSGLGAMGF GLPAAIGASV ANPDAIVVDI DGDGSFIMNV QELATIRVEN 550 560 570 580 590 600 LPVKILLLNN QHLGMVMQWE DRFYKANRAH TYLGDPAREN EIFPNMLQFA GACGIPAARV 610 620 630 640 650 TKKEELREAI QTMLDTPGPY LLDVICPHQE HVLPMIPSGG TFKDVITEGD GRTKY

References

[1]	"Molecular characterization and genetic origin of the Brassica napus acetohydroxyacid synthase multigene family." Rutledge R.G., Ouellet T., Hattori J., Miki B.L.A. Mol. Gen. Genet. 229:31-40(1991) [PubMed: 1896019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Topas.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z11524 Genomic DNA. Translation: CAA77613.1.
PIR	S17691.
3D structure databases
HSSP	HSSP built from PDB template 1JSC based on UniProtKB P07342.
SMR	P27818. Positions 71-652.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.2.1.6. 393.
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

ILVB1_BRANA

Accession

Primary (citable) accession number: P27818

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)