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Protein

Acetolactate synthase, chloroplastic

Gene

ALS

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis.9 Publications

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by asymmetric aryl disulfides, triazolopyrimidine sulfonanilide compounds, isatin derivatives, and sulfonylurea and imidazolinone herbicides. Insensitive to feed-back inhibition by branched-chain amino acids.5 Publications

pH dependencei

Optimum pH is 7.0-7.5.2 Publications

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441Thiamine pyrophosphate1 Publication
Binding sitei207 – 2071Thiamine pyrophosphate1 Publication
Binding sitei220 – 2201Imidazolinone herbicides
Binding sitei246 – 2461FAD1 Publication
Binding sitei246 – 2461Imidazolinone herbicides; via amide nitrogen
Binding sitei256 – 2561Sulfonylurea herbicides1 Publication
Binding sitei308 – 3081FAD; via amide nitrogen1 Publication
Binding sitei377 – 3771Imidazolinone and sulfonylurea herbicides
Metal bindingi538 – 5381Magnesium2 Publications
Metal bindingi565 – 5651Magnesium2 Publications
Metal bindingi567 – 5671Magnesium; via carbonyl oxygen2 Publications
Binding sitei574 – 5741Sulfonylurea herbicides1 Publication
Binding sitei653 – 6531Sulfonylurea herbicides1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi331 – 3322FAD1 Publication
Nucleotide bindingi349 – 3524FAD1 Publication
Nucleotide bindingi371 – 3755FAD1 Publication
Nucleotide bindingi395 – 3962FAD1 Publication
Nucleotide bindingi414 – 4152FAD1 Publication
Nucleotide bindingi508 – 5092FAD1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Herbicide resistance

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciARA:AT3G48560-MONOMER.
BRENDAi2.2.1.6. 399.
SABIO-RKP17597.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase, chloroplastic (EC:2.2.1.6)
Short name:
AtALS
Alternative name(s):
Acetohydroxy-acid synthase
Protein CHLORSULFURON RESISTANT 1
Gene namesi
Name:ALS
Synonyms:AHAS, CSR1, TZP5
Ordered Locus Names:At3g48560
ORF Names:T8P19.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G48560.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Biotechnological usei

Introduced by genetic manipulation and expressed in sulfonylurea resistant plants.

Disruption phenotypei

Lethal when homozygous.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221A → V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 1 Publication
Mutagenesisi124 – 1241M → E: Reduced catalytic activity. Resistant to imidazolinone herbicides and reduced sensitivity to sulfonylurea herbicides. 1 Publication
Mutagenesisi124 – 1241M → I: No effect on catalytic activity. Increased resistance to imidazolinone herbicides. 1 Publication
Mutagenesisi197 – 1971P → S in csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides. 1 Publication
Mutagenesisi199 – 1991R → A or E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 1 Publication
Mutagenesisi574 – 5741W → L: Increased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. 1 Publication
Mutagenesisi574 – 5741W → S: Slightly decreased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. 1 Publication
Mutagenesisi653 – 6531S → A: No effect on catalytic activity or sensitivity to herbicides. 4 Publications
Mutagenesisi653 – 6531S → F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant. 4 Publications
Mutagenesisi653 – 6531S → N in csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides. 4 Publications
Mutagenesisi653 – 6531S → T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 4 Publications

Chemistry

ChEMBLiCHEMBL4263.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555ChloroplastSequence analysisAdd
BLAST
Chaini56 – 670615Acetolactate synthase, chloroplasticPRO_0000035655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei340 – 3401Cysteine sulfinic acid (-SO2H)2 Publications

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiP17597.
PRIDEiP17597.

Expressioni

Gene expression databases

GenevisibleiP17597. AT.

Interactioni

Subunit structurei

Homodimer or homotetramer. The acetolactate synthase complex contains both large catalytic subunits and small regulatory subunits.3 Publications

Protein-protein interaction databases

BioGridi9334. 1 interaction.
DIPiDIP-61092N.
STRINGi3702.AT3G48560.1.

Chemistry

BindingDBiP17597.

Structurei

Secondary structure

1
670
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi99 – 10810Combined sources
Turni109 – 1113Combined sources
Beta strandi114 – 1174Combined sources
Helixi121 – 1233Combined sources
Helixi124 – 1329Combined sources
Helixi144 – 15815Combined sources
Beta strandi162 – 1665Combined sources
Helixi170 – 1734Combined sources
Helixi176 – 18510Combined sources
Beta strandi189 – 1957Combined sources
Helixi198 – 2003Combined sources
Turni201 – 2044Combined sources
Helixi211 – 2155Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2246Combined sources
Helixi228 – 2303Combined sources
Helixi231 – 24313Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi249 – 2557Combined sources
Helixi256 – 2605Combined sources
Helixi274 – 2796Combined sources
Helixi286 – 29813Combined sources
Beta strandi300 – 3067Combined sources
Helixi308 – 3103Combined sources
Helixi314 – 32411Combined sources
Beta strandi328 – 3303Combined sources
Turni332 – 3365Combined sources
Beta strandi340 – 3423Combined sources
Beta strandi345 – 3484Combined sources
Helixi355 – 3639Combined sources
Beta strandi365 – 3717Combined sources
Helixi376 – 3794Combined sources
Helixi382 – 3843Combined sources
Turni385 – 3884Combined sources
Beta strandi389 – 3968Combined sources
Turni398 – 4025Combined sources
Beta strandi403 – 4053Combined sources
Beta strandi408 – 4136Combined sources
Helixi415 – 42814Combined sources
Helixi430 – 4334Combined sources
Helixi438 – 45013Combined sources
Helixi464 – 47512Combined sources
Beta strandi480 – 4834Combined sources
Helixi487 – 4948Combined sources
Beta strandi503 – 5053Combined sources
Helixi516 – 52611Combined sources
Beta strandi532 – 5376Combined sources
Helixi538 – 5436Combined sources
Helixi544 – 5463Combined sources
Helixi547 – 5537Combined sources
Beta strandi558 – 5647Combined sources
Helixi569 – 57810Combined sources
Helixi591 – 5933Combined sources
Helixi601 – 6077Combined sources
Beta strandi612 – 6154Combined sources
Helixi618 – 63013Combined sources
Beta strandi631 – 6333Combined sources
Beta strandi635 – 6406Combined sources
Beta strandi648 – 6503Combined sources
Helixi657 – 6593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP17597.
SMRiP17597. Positions 86-667.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17597.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni376 – 3772Sulfonylurea herbicides binding
Regioni487 – 4882Thiamine pyrophosphate binding
Regioni511 – 5133Thiamine pyrophosphate binding
Regioni538 – 5403Thiamine pyrophosphate binding
Regioni565 – 5706Thiamine pyrophosphate binding

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili414 – 44633Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiKOG4166. Eukaryota.
COG0028. LUCA.
HOGENOMiHOG000258448.
InParanoidiP17597.
KOiK01652.
OMAiHSWVVRD.
PhylomeDBiP17597.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17597-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATTTTTT SSSISFSTKP SPSSSKSPLP ISRFSLPFSL NPNKSSSSSR
60 70 80 90 100
RRGIKSSSPS SISAVLNTTT NVTTTPSPTK PTKPETFISR FAPDQPRKGA
110 120 130 140 150
DILVEALERQ GVETVFAYPG GASMEIHQAL TRSSSIRNVL PRHEQGGVFA
160 170 180 190 200
AEGYARSSGK PGICIATSGP GATNLVSGLA DALLDSVPLV AITGQVPRRM
210 220 230 240 250
IGTDAFQETP IVEVTRSITK HNYLVMDVED IPRIIEEAFF LATSGRPGPV
260 270 280 290 300
LVDVPKDIQQ QLAIPNWEQA MRLPGYMSRM PKPPEDSHLE QIVRLISESK
310 320 330 340 350
KPVLYVGGGC LNSSDELGRF VELTGIPVAS TLMGLGSYPC DDELSLHMLG
360 370 380 390 400
MHGTVYANYA VEHSDLLLAF GVRFDDRVTG KLEAFASRAK IVHIDIDSAE
410 420 430 440 450
IGKNKTPHVS VCGDVKLALQ GMNKVLENRA EELKLDFGVW RNELNVQKQK
460 470 480 490 500
FPLSFKTFGE AIPPQYAIKV LDELTDGKAI ISTGVGQHQM WAAQFYNYKK
510 520 530 540 550
PRQWLSSGGL GAMGFGLPAA IGASVANPDA IVVDIDGDGS FIMNVQELAT
560 570 580 590 600
IRVENLPVKV LLLNNQHLGM VMQWEDRFYK ANRAHTFLGD PAQEDEIFPN
610 620 630 640 650
MLLFAAACGI PAARVTKKAD LREAIQTMLD TPGPYLLDVI CPHQEHVLPM
660 670
IPSGGTFNDV ITEGDGRIKY
Length:670
Mass (Da):72,585
Last modified:August 1, 1990 - v1
Checksum:iDA697A8DD155F160
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041V → A in ABJ80681 (Ref. 8) Curated
Sequence conflicti161 – 1611P → S in ABJ80681 (Ref. 8) Curated
Sequence conflicti208 – 2081E → G in ABJ80681 (Ref. 8) Curated
Sequence conflicti466 – 4661Y → H in ABJ80681 (Ref. 8) Curated
Sequence conflicti555 – 5551N → Q in AAM92569 (Ref. 5) Curated
Sequence conflicti560 – 5601V → I in AAM92569 (Ref. 5) Curated
Sequence conflicti575 – 5751E → Q in AAK68759 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51514 Genomic DNA. Translation: CAA35887.1.
AL133315 Genomic DNA. Translation: CAB62345.1.
CP002686 Genomic DNA. Translation: AEE78430.1.
AY124092 Genomic DNA. Translation: AAM92569.1.
AY042819 mRNA. Translation: AAK68759.1.
BT020540 mRNA. Translation: AAW70386.1.
DQ991161 mRNA. Translation: ABJ80681.1.
PIRiS09502. YCMU.
RefSeqiNP_190425.1. NM_114714.2.
UniGeneiAt.22295.
At.72000.

Genome annotation databases

EnsemblPlantsiAT3G48560.1; AT3G48560.1; AT3G48560.
GeneIDi824015.
GrameneiAT3G48560.1; AT3G48560.1; AT3G48560.
KEGGiath:AT3G48560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51514 Genomic DNA. Translation: CAA35887.1.
AL133315 Genomic DNA. Translation: CAB62345.1.
CP002686 Genomic DNA. Translation: AEE78430.1.
AY124092 Genomic DNA. Translation: AAM92569.1.
AY042819 mRNA. Translation: AAK68759.1.
BT020540 mRNA. Translation: AAW70386.1.
DQ991161 mRNA. Translation: ABJ80681.1.
PIRiS09502. YCMU.
RefSeqiNP_190425.1. NM_114714.2.
UniGeneiAt.22295.
At.72000.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP17597.
SMRiP17597. Positions 86-667.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9334. 1 interaction.
DIPiDIP-61092N.
STRINGi3702.AT3G48560.1.

Chemistry

BindingDBiP17597.
ChEMBLiCHEMBL4263.

Proteomic databases

PaxDbiP17597.
PRIDEiP17597.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G48560.1; AT3G48560.1; AT3G48560.
GeneIDi824015.
GrameneiAT3G48560.1; AT3G48560.1; AT3G48560.
KEGGiath:AT3G48560.

Organism-specific databases

TAIRiAT3G48560.

Phylogenomic databases

eggNOGiKOG4166. Eukaryota.
COG0028. LUCA.
HOGENOMiHOG000258448.
InParanoidiP17597.
KOiK01652.
OMAiHSWVVRD.
PhylomeDBiP17597.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.
BioCyciARA:AT3G48560-MONOMER.
BRENDAi2.2.1.6. 399.
SABIO-RKP17597.

Miscellaneous databases

EvolutionaryTraceiP17597.
PROiP17597.

Gene expression databases

GenevisibleiP17597. AT.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of plant genes coding for acetolactate synthase, the target enzyme for two classes of herbicides."
    Mazur B.J., Chui C.F., Smith J.K.
    Plant Physiol. 85:1110-1117(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-653, FUNCTION.
    Strain: cv. Columbia.
  3. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Saturation mutagenesis in Arabidopsis to determine frequency of herbicide resistance."
    Jander G., Baerson S.R., Hudak J.A., Gonzalez K.A., Gruys K.J., Last R.L.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "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.
  8. "Cloning of Arabidopsis thaliana acetolactate synthase catalytic subunit."
    Jiang L., Xiang W., Wang X., Wang X., Zhang J., Xi D., Gao A.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  9. "Transformation with a mutant Arabidopsis acetolactate synthase gene renders tobacco resistant to sulfonylurea herbicides."
    Haughn G.W., Smith J.K., Mazur B.J., Somerville C.
    Mol. Gen. Genet. 211:266-271(1988)
    Cited for: FUNCTION, MUTAGENESIS OF PRO-197.
    Strain: cv. Columbia.
  10. "A mutation causing imidazolinone resistance maps to the csr1 locus of Arabidopsis thaliana."
    Haughn G.W., Somerville C.R.
    Plant Physiol. 92:1081-1085(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-653.
    Strain: cv. Columbia.
  12. "Rational molecular design and genetic engineering of herbicide resistant crops by structure modeling and site-directed mutagenesis of acetohydroxyacid synthase."
    Ott K.H., Kwagh J.G., Stockton G.W., Sidorov V., Kakefuda G.
    J. Mol. Biol. 263:359-368(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, FUNCTION, MUTAGENESIS OF MET-124 AND ARG-199.
  13. "Expression, purification and characterization of Arabidopsis thaliana acetohydroxyacid synthase."
    Chang A.K., Duggleby R.G.
    Biochem. J. 327:161-169(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, SUBUNIT.
  14. "Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid synthase: characterization of the catalytic properties and sensitivity to inhibitors of four defined mutants."
    Chang A.K., Duggleby R.G.
    Biochem. J. 333:765-777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF ALA-122; TRP-574 AND SER-653.
  15. "Effect of mutagenesis at serine 653 of Arabidopsis thaliana acetohydroxyacid synthase on the sensitivity to imidazolinone and sulfonylurea herbicides."
    Lee Y.T., Chang A.K., Duggleby R.G.
    FEBS Lett. 452:341-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-653.
  16. "Design and synthesis of N-2,6-difluorophenyl-5-methoxyl-1,2,4-triazolo[1,5-a]-pyrimidine-2-sulfonamide as acetohydroxyacid synthase inhibitor."
    Chen C.N., Lv L.L., Ji F.Q., Chen Q., Xu H., Niu C.W., Xi Z., Yang G.F.
    Bioorg. Med. Chem. 17:3011-3017(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
  17. "Syntheses and herbicidal activity of new triazolopyrimidine-2-sulfonamides as acetohydroxyacid synthase inhibitor."
    Chen C.N., Chen Q., Liu Y.C., Zhu X.L., Niu C.W., Xi Z., Yang G.F.
    Bioorg. Med. Chem. 18:4897-4904(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
  18. "Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition, herbicidal activity, and computational studies of isatin derivatives."
    Wang J., Tan H., Li Y., Ma Y., Li Z., Guddat L.W.
    J. Agric. Food Chem. 59:9892-9900(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
  19. "Synthesis, crystal structure, in vitro acetohydroxyacid synthase inhibition, in vivo herbicidal activity, and 3D-QSAR of new asymmetric aryl disulfides."
    Shang J., Wang W.M., Li Y.H., Song H.B., Li Z.M., Wang J.G.
    J. Agric. Food Chem. 60:8286-8293(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ENZYME REGULATION.
  20. "Comparability of imazapyr-resistant Arabidopsis created by transgenesis and mutagenesis."
    Schnell J., Labbe H., Kovinich N., Manabe Y., Miki B.
    Transgenic Res. 21:1255-1264(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  21. "Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase."
    McCourt J.A., Pang S.S., King-Scott J., Guddat L.W., Duggleby R.G.
    Proc. Natl. Acad. Sci. U.S.A. 103:569-573(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 86-667 IN COMPLEX WITH FAD; MAGNESIUM; THIAMINE PYROPHOSPHATE AND HERBICIDES, OXIDATION AT CYS-340, SUBUNIT.
  22. "Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase."
    Wang J.G., Lee P.K., Dong Y.H., Pang S.S., Duggleby R.G., Li Z.M., Guddat L.W.
    FEBS J. 276:1282-1290(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 87-670 IN COMPLEX WITH MAGNESIUM AND SULFONYLUREA HERBICIDES, OXIDATION AT CYS-340.

Entry informationi

Entry nameiILVB_ARATH
AccessioniPrimary (citable) accession number: P17597
Secondary accession number(s): A0A174
, Q5FV34, Q8L7Y7, Q94B64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 17, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Genetically modified food, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.