Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P27818 (ILVB1_BRANA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetolactate synthase 1, chloroplastic

EC=2.2.1.6
Alternative name(s):
ALS I
Acetohydroxy-acid synthase I
Acetolactate synthase I
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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

Plastidchloroplast.

Miscellaneous

Acetolactate synthase is the target enzyme for sulfonylurea and imidazolinone herbicides.

Sequence similarities

Belongs to the TPP enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8282Chloroplast By similarity
Chain83 – 655573Acetolactate synthase 1, chloroplastic
PRO_0000035656

Regions

Nucleotide binding337 – 35822FAD By similarity
Nucleotide binding380 – 39920FAD By similarity
Region472 – 55281Thiamine pyrophosphate binding

Sites

Metal binding5231Magnesium By similarity
Metal binding5501Magnesium By similarity
Binding site1291Thiamine pyrophosphate By similarity
Binding site2311FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P27818 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 1BEAD7D7A0DAD91A

FASTA65571,289
        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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Topas.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11524 Genomic DNA. Translation: CAA77613.1.
PIRS17691.

3D structure databases

ProteinModelPortalP27818.
SMRP27818. Positions 71-652.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00047; UER00055.
UPA00049; UER00059.

Family and domain databases

InterProIPR012846. 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]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00118. acolac_lg. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameILVB1_BRANA
AccessionPrimary (citable) accession number: P27818
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways