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P17597 (ILVB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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, chloroplastic
EC=2.2.1.6
Alternative name(s):
ALS
Acetohydroxy-acid synthase
Gene names
Name:CSR 1.2
Ordered Locus Names:At3g48560
ORF Names:T8P19.70
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Biotechnological use

Introduced by genetic manipulation and expressed in sulfonylurea resistant flax by the University of Saskatchewan.

Miscellaneous

Acetolactate synthase is the target enzyme for sulfonylurea and imidazolinone herbicides. Mutant GH 90 is resistant to imidazolinone herbicides and mutant GH 50 to sulfonylurea.

Sequence similarities

Belongs to the TPP enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9797Chloroplast
Chain98 – 670573Acetolactate synthase, chloroplastic
PRO_0000035655

Regions

Nucleotide binding352 – 37322FAD By similarity
Nucleotide binding395 – 41420FAD By similarity
Region487 – 56781Thiamine pyrophosphate binding

Sites

Metal binding5381Magnesium By similarity
Metal binding5651Magnesium By similarity
Binding site1441Thiamine pyrophosphate By similarity
Binding site2461FAD By similarity

Natural variations

Natural variant1971P → S in mutant GH 50.
Natural variant6531S → N in mutant GH 90.

Secondary structure

1 ...................................................................................................... 670
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17597 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: DA697A8DD155F160

FASTA67072,585
        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

« Hide

References

« Hide 'large scale' references
[1]"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: 2336405] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"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. expand/collapse author list , 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: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
[5]"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: 16668488] [Abstract]
Cited for: VARIANT GH90.
Strain: cv. Columbia.
+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.
BT020540 mRNA. Translation: AAW70386.1.
IPIIPI00522536.
PIRYCMU. S09502.
RefSeqNP_190425.1. NM_114714.2.
UniGeneAt.22295.
At.71451.
At.72000.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YBHX-ray2.50A86-667[»]
1YHYX-ray2.70A86-667[»]
1YHZX-ray2.70A86-667[»]
1YI0X-ray2.70A86-667[»]
1YI1X-ray2.90A86-667[»]
1Z8NX-ray2.80A86-667[»]
3E9YX-ray3.00A87-670[»]
3EA4X-ray2.80A87-670[»]
ProteinModelPortalP17597.
SMRP17597. Positions 86-667.
ModBaseSearch...

Protein-protein interaction databases

STRINGP17597.

Proteomic databases

PRIDEP17597.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G48560.1; AT3G48560.1; AT3G48560.
GeneID824015.
GenomeReviewsGene locus AT3G48560 in contig BA000014_GR.
KEGGath:AT3G48560.
NMPDRfig|3702.1.peg.16095.

Organism-specific databases

TAIRAt3g48560.

Phylogenomic databases

HOGENOMHBG323037.
InParanoidP17597.
OMAMVLINNQ.
PhylomeDBP17597.
ProtClustDBPLN02470.

Gene expression databases

ArrayExpressP17597.
GenevestigatorP17597.
GermOnlineAT3G48560. Arabidopsis thaliana.

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]
KOK01652.
PANTHERPTHR18968:SF13. PTHR18968:SF13. 1 hit.
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 nameILVB_ARATH
AccessionPrimary (citable) accession number: P17597
Secondary accession number(s): Q5FV34
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: January 25, 2012
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents