Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 (AXX17_At3g42690), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150)
  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 (AXX17_At3g42690), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150)
  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)DescriptionActionsGraphical viewLength
Binding sitei144Thiamine pyrophosphate1 Publication1
Binding sitei207Thiamine pyrophosphate1 Publication1
Binding sitei220Imidazolinone herbicides1
Binding sitei246FAD1 Publication1
Binding sitei246Imidazolinone herbicides; via amide nitrogen1
Binding sitei256Sulfonylurea herbicides1 Publication1
Binding sitei308FAD; via amide nitrogen1 Publication1
Binding sitei377Imidazolinone and sulfonylurea herbicides1
Metal bindingi538Magnesium2 Publications1
Metal bindingi565Magnesium2 Publications1
Metal bindingi567Magnesium; via carbonyl oxygen2 Publications1
Binding sitei574Sulfonylurea herbicides1 Publication1
Binding sitei653Sulfonylurea herbicides1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi331 – 332FAD1 Publication2
Nucleotide bindingi349 – 352FAD1 Publication4
Nucleotide bindingi371 – 375FAD1 Publication5
Nucleotide bindingi395 – 396FAD1 Publication2
Nucleotide bindingi414 – 415FAD1 Publication2
Nucleotide bindingi508 – 509FAD1 Publication2

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)DescriptionActionsGraphical viewLength
Mutagenesisi122A → V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 1 Publication1
Mutagenesisi124M → E: Reduced catalytic activity. Resistant to imidazolinone herbicides and reduced sensitivity to sulfonylurea herbicides. 1 Publication1
Mutagenesisi124M → I: No effect on catalytic activity. Increased resistance to imidazolinone herbicides. 1 Publication1
Mutagenesisi197P → S in csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides. 1 Publication1
Mutagenesisi199R → A or E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 1 Publication1
Mutagenesisi574W → L: Increased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. 1 Publication1
Mutagenesisi574W → S: Slightly decreased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. 1 Publication1
Mutagenesisi653S → A: No effect on catalytic activity or sensitivity to herbicides. 4 Publications1
Mutagenesisi653S → F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant. 4 Publications1
Mutagenesisi653S → N in csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides. 4 Publications1
Mutagenesisi653S → T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 4 Publications1

Chemistry databases

ChEMBLiCHEMBL4263.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 55ChloroplastSequence analysisAdd BLAST55
ChainiPRO_000003565556 – 670Acetolactate synthase, chloroplasticAdd BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei340Cysteine sulfinic acid (-SO2H)2 Publications1

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 interactor.
DIPiDIP-61092N.
STRINGi3702.AT3G48560.1.

Chemistry databases

BindingDBiP17597.

Structurei

Secondary structure

1670
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi99 – 108Combined sources10
Turni109 – 111Combined sources3
Beta strandi114 – 117Combined sources4
Helixi121 – 123Combined sources3
Helixi124 – 132Combined sources9
Helixi144 – 158Combined sources15
Beta strandi162 – 166Combined sources5
Helixi170 – 173Combined sources4
Helixi176 – 185Combined sources10
Beta strandi189 – 195Combined sources7
Helixi198 – 200Combined sources3
Turni201 – 204Combined sources4
Helixi211 – 215Combined sources5
Helixi216 – 218Combined sources3
Beta strandi219 – 224Combined sources6
Helixi228 – 230Combined sources3
Helixi231 – 243Combined sources13
Beta strandi244 – 246Combined sources3
Beta strandi249 – 255Combined sources7
Helixi256 – 260Combined sources5
Helixi274 – 279Combined sources6
Helixi286 – 298Combined sources13
Beta strandi300 – 306Combined sources7
Helixi308 – 310Combined sources3
Helixi314 – 324Combined sources11
Beta strandi328 – 330Combined sources3
Turni332 – 336Combined sources5
Beta strandi340 – 342Combined sources3
Beta strandi345 – 348Combined sources4
Helixi355 – 363Combined sources9
Beta strandi365 – 371Combined sources7
Helixi376 – 379Combined sources4
Helixi382 – 384Combined sources3
Turni385 – 388Combined sources4
Beta strandi389 – 396Combined sources8
Turni398 – 402Combined sources5
Beta strandi403 – 405Combined sources3
Beta strandi408 – 413Combined sources6
Helixi415 – 428Combined sources14
Helixi430 – 433Combined sources4
Helixi438 – 450Combined sources13
Helixi464 – 475Combined sources12
Beta strandi480 – 483Combined sources4
Helixi487 – 494Combined sources8
Beta strandi503 – 505Combined sources3
Helixi516 – 526Combined sources11
Beta strandi532 – 537Combined sources6
Helixi538 – 543Combined sources6
Helixi544 – 546Combined sources3
Helixi547 – 553Combined sources7
Beta strandi558 – 564Combined sources7
Helixi569 – 578Combined sources10
Helixi591 – 593Combined sources3
Helixi601 – 607Combined sources7
Beta strandi612 – 615Combined sources4
Helixi618 – 630Combined sources13
Beta strandi631 – 633Combined sources3
Beta strandi635 – 640Combined sources6
Beta strandi648 – 650Combined sources3
Helixi657 – 659Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17597.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni376 – 377Sulfonylurea herbicides binding2
Regioni487 – 488Thiamine pyrophosphate binding2
Regioni511 – 513Thiamine pyrophosphate binding3
Regioni538 – 540Thiamine pyrophosphate binding3
Regioni565 – 570Thiamine pyrophosphate binding6

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili414 – 446Sequence analysisAdd BLAST33

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.
OrthoDBiEOG0936048A.
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)DescriptionActionsGraphical viewLength
Sequence conflicti104V → A in ABJ80681 (Ref. 8) Curated1
Sequence conflicti161P → S in ABJ80681 (Ref. 8) Curated1
Sequence conflicti208E → G in ABJ80681 (Ref. 8) Curated1
Sequence conflicti466Y → H in ABJ80681 (Ref. 8) Curated1
Sequence conflicti555N → Q in AAM92569 (Ref. 5) Curated1
Sequence conflicti560V → I in AAM92569 (Ref. 5) Curated1
Sequence conflicti575E → Q in AAK68759 (PubMed:14593172).Curated1

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_114714.3.
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_114714.3.
UniGeneiAt.22295.
At.72000.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

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.
OrthoDBiEOG0936048A.
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...

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: November 30, 2016
This is version 160 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.