UniProtKB - P17597 (ILVB_ARATH)
Protein
Acetolactate synthase, chloroplastic
Gene
ALS
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Functioni
Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis.9 Publications
Catalytic activityi
- EC:2.2.1.6
Cofactori
Protein has several cofactor binding sites:- Mg2+Note: Binds 1 Mg2+ ion per subunit.
- FAD
- thiamine diphosphateNote: Binds 1 thiamine pyrophosphate per subunit.
Activity 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
: L-isoleucine biosynthesis Pathwayi
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:
- Acetolactate synthase, chloroplastic (ALS), Acetohydroxy-acid synthase small subunit (At5g16290), Acetolactate synthase (AXX17_At3g42690), Acetolactate synthase (AN1_LOCUS15201), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetohydroxy-acid synthase small subunit (AN1_LOCUS22406), Acetohydroxy-acid synthase small subunit (AXX17_At2g28020), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
- Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150), Acetohydroxy-acid reductoisomerase (At3g58610), Ketol-acid reductoisomerase (At3g58610)
- Dihydroxy-acid dehydratase, chloroplastic (DHAD)
- Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
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:
- Acetolactate synthase, chloroplastic (ALS), Acetohydroxy-acid synthase small subunit (At5g16290), Acetolactate synthase (AXX17_At3g42690), Acetolactate synthase (AN1_LOCUS15201), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetohydroxy-acid synthase small subunit (AN1_LOCUS22406), Acetohydroxy-acid synthase small subunit (AXX17_At2g28020), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
- Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150), Acetohydroxy-acid reductoisomerase (At3g58610), Ketol-acid reductoisomerase (At3g58610)
- Dihydroxy-acid dehydratase, chloroplastic (DHAD)
- Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 144 | Thiamine pyrophosphate1 Publication | 1 | |
Binding sitei | 207 | Thiamine pyrophosphate1 Publication | 1 | |
Binding sitei | 220 | Imidazolinone herbicides | 1 | |
Binding sitei | 246 | FAD1 Publication | 1 | |
Binding sitei | 246 | Imidazolinone herbicides; via amide nitrogen | 1 | |
Binding sitei | 256 | Sulfonylurea herbicides1 Publication | 1 | |
Binding sitei | 308 | FAD; via amide nitrogen1 Publication | 1 | |
Binding sitei | 377 | Imidazolinone and sulfonylurea herbicides | 1 | |
Metal bindingi | 538 | Magnesium2 Publications | 1 | |
Metal bindingi | 565 | Magnesium2 Publications | 1 | |
Metal bindingi | 567 | Magnesium; via carbonyl oxygen2 Publications | 1 | |
Binding sitei | 574 | Sulfonylurea herbicides1 Publication | 1 | |
Binding sitei | 653 | Sulfonylurea herbicides1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 331 – 332 | FAD1 Publication | 2 | |
Nucleotide bindingi | 349 – 352 | FAD1 Publication | 4 | |
Nucleotide bindingi | 371 – 375 | FAD1 Publication | 5 | |
Nucleotide bindingi | 395 – 396 | FAD1 Publication | 2 | |
Nucleotide bindingi | 414 – 415 | FAD1 Publication | 2 | |
Nucleotide bindingi | 508 – 509 | FAD1 Publication | 2 |
GO - Molecular functioni
- acetolactate synthase activity Source: TAIR
- flavin adenine dinucleotide binding Source: GO_Central
- magnesium ion binding Source: InterPro
- thiamine pyrophosphate binding Source: InterPro
GO - Biological processi
- isoleucine biosynthetic process Source: GO_Central
- response to herbicide Source: UniProtKB-KW
- valine biosynthetic process Source: TAIR
Keywordsi
Molecular function | Transferase |
Biological process | Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Herbicide resistance |
Ligand | FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyci | ARA:AT3G48560-MONOMER |
BRENDAi | 2.2.1.6, 399 |
SABIO-RKi | P17597 |
UniPathwayi | UPA00047;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 |
Organismi | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic identifieri | 3702 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Proteomesi |
|
Organism-specific databases
Araporti | AT3G48560 |
TAIRi | locus:2114525, AT3G48560 |
Subcellular locationi
Chloroplast
- chloroplast Curated
Chloroplast
- chloroplast Source: TAIR
- chloroplast stroma Source: TAIR
Other locations
- acetolactate synthase complex Source: GO_Central
Keywords - Cellular componenti
Chloroplast, PlastidPathology & Biotechi
Biotechnological usei
Introduced by genetic manipulation and expressed in sulfonylurea resistant plants.
Disruption phenotypei
Lethal when homozygous.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 122 | A → V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 1 Publication | 1 | |
Mutagenesisi | 124 | M → E: Reduced catalytic activity. Resistant to imidazolinone herbicides and reduced sensitivity to sulfonylurea herbicides. 1 Publication | 1 | |
Mutagenesisi | 124 | M → I: No effect on catalytic activity. Increased resistance to imidazolinone herbicides. 1 Publication | 1 | |
Mutagenesisi | 197 | P → S in csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides. 1 Publication | 1 | |
Mutagenesisi | 199 | R → A or E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 1 Publication | 1 | |
Mutagenesisi | 574 | W → L: Increased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. 1 Publication | 1 | |
Mutagenesisi | 574 | W → S: Slightly decreased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides. 1 Publication | 1 | |
Mutagenesisi | 653 | S → A: No effect on catalytic activity or sensitivity to herbicides. 4 Publications | 1 | |
Mutagenesisi | 653 | S → F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant. 4 Publications | 1 | |
Mutagenesisi | 653 | S → N in csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides. 4 Publications | 1 | |
Mutagenesisi | 653 | S → T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides. 4 Publications | 1 |
Chemistry databases
ChEMBLi | CHEMBL4263 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 55 | ChloroplastSequence analysisAdd BLAST | 55 | |
ChainiPRO_0000035655 | 56 – 670 | Acetolactate synthase, chloroplasticAdd BLAST | 615 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 340 | Cysteine sulfinic acid (-SO2H)2 Publications | 1 |
Keywords - PTMi
OxidationProteomic databases
PaxDbi | P17597 |
PRIDEi | P17597 |
ProteomicsDBi | 228865 |
PTM databases
MetOSitei | P17597 |
Expressioni
Gene expression databases
ExpressionAtlasi | P17597, baseline and differential |
Genevisiblei | P17597, AT |
Interactioni
Subunit structurei
Homodimer or homotetramer. The acetolactate synthase complex contains both large catalytic subunits and small regulatory subunits.
3 PublicationsProtein-protein interaction databases
BioGRIDi | 9334, 1 interactor |
DIPi | DIP-61092N |
STRINGi | 3702.AT3G48560.1 |
Chemistry databases
BindingDBi | P17597 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P17597 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P17597 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 376 – 377 | Sulfonylurea herbicides binding | 2 | |
Regioni | 487 – 488 | Thiamine pyrophosphate binding | 2 | |
Regioni | 511 – 513 | Thiamine pyrophosphate binding | 3 | |
Regioni | 538 – 540 | Thiamine pyrophosphate binding | 3 | |
Regioni | 565 – 570 | Thiamine pyrophosphate binding | 6 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 414 – 446 | Sequence analysisAdd BLAST | 33 |
Sequence similaritiesi
Belongs to the TPP enzyme family.Curated
Keywords - Domaini
Coiled coil, Transit peptidePhylogenomic databases
eggNOGi | KOG4166, Eukaryota |
HOGENOMi | CLU_013748_1_2_1 |
InParanoidi | P17597 |
OMAi | MRSYNPV |
OrthoDBi | 1132247at2759 |
PhylomeDBi | P17597 |
Family and domain databases
CDDi | cd02015, TPP_AHAS, 1 hit |
InterProi | View protein in InterPro IPR012846, Acetolactate_synth_lsu IPR039368, AHAS_TPP 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 |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF00205, TPP_enzyme_M, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00118, acolac_lg, 1 hit |
PROSITEi | View protein in PROSITE PS00187, TPP_ENZYMES, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P17597-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 104 | V → A in ABJ80681 (Ref. 8) Curated | 1 | |
Sequence conflicti | 161 | P → S in ABJ80681 (Ref. 8) Curated | 1 | |
Sequence conflicti | 208 | E → G in ABJ80681 (Ref. 8) Curated | 1 | |
Sequence conflicti | 466 | Y → H in ABJ80681 (Ref. 8) Curated | 1 | |
Sequence conflicti | 555 | N → Q in AAM92569 (Ref. 5) Curated | 1 | |
Sequence conflicti | 560 | V → I in AAM92569 (Ref. 5) Curated | 1 | |
Sequence conflicti | 575 | E → Q in AAK68759 (PubMed:14593172).Curated | 1 |
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 |
PIRi | S09502, YCMU |
RefSeqi | NP_190425.1, NM_114714.3 |
Genome annotation databases
EnsemblPlantsi | AT3G48560.1; AT3G48560.1; AT3G48560 |
GeneIDi | 824015 |
Gramenei | AT3G48560.1; AT3G48560.1; AT3G48560 |
KEGGi | ath:AT3G48560 |
Similar proteinsi
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 |
PIRi | S09502, YCMU |
RefSeqi | NP_190425.1, NM_114714.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1YBH | X-ray | 2.50 | A | 86-667 | [»] | |
1YHY | X-ray | 2.70 | A | 86-667 | [»] | |
1YHZ | X-ray | 2.70 | A | 86-667 | [»] | |
1YI0 | X-ray | 2.70 | A | 86-667 | [»] | |
1YI1 | X-ray | 2.90 | A | 86-667 | [»] | |
1Z8N | X-ray | 2.80 | A | 86-667 | [»] | |
3E9Y | X-ray | 3.00 | A | 87-670 | [»] | |
3EA4 | X-ray | 2.80 | A | 87-670 | [»] | |
5K2O | X-ray | 2.87 | A | 86-667 | [»] | |
5K3S | X-ray | 2.87 | A | 86-667 | [»] | |
5K6Q | X-ray | 2.95 | A | 86-667 | [»] | |
5K6R | X-ray | 2.73 | A | 86-667 | [»] | |
5K6T | X-ray | 2.76 | A | 86-667 | [»] | |
5WJ1 | X-ray | 2.52 | A | 86-667 | [»] | |
6U9H | electron microscopy | 3.80 | A/B/H/I/L/M/P/Q | 86-670 | [»] | |
6VZ8 | electron microscopy | 3.45 | D/E/H/I/L/M/P/Q | 86-670 | [»] | |
SMRi | P17597 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 9334, 1 interactor |
DIPi | DIP-61092N |
STRINGi | 3702.AT3G48560.1 |
Chemistry databases
BindingDBi | P17597 |
ChEMBLi | CHEMBL4263 |
PTM databases
MetOSitei | P17597 |
Proteomic databases
PaxDbi | P17597 |
PRIDEi | P17597 |
ProteomicsDBi | 228865 |
Genome annotation databases
EnsemblPlantsi | AT3G48560.1; AT3G48560.1; AT3G48560 |
GeneIDi | 824015 |
Gramenei | AT3G48560.1; AT3G48560.1; AT3G48560 |
KEGGi | ath:AT3G48560 |
Organism-specific databases
Araporti | AT3G48560 |
TAIRi | locus:2114525, AT3G48560 |
Phylogenomic databases
eggNOGi | KOG4166, Eukaryota |
HOGENOMi | CLU_013748_1_2_1 |
InParanoidi | P17597 |
OMAi | MRSYNPV |
OrthoDBi | 1132247at2759 |
PhylomeDBi | P17597 |
Enzyme and pathway databases
UniPathwayi | UPA00047;UER00055 UPA00049;UER00059 |
BioCyci | ARA:AT3G48560-MONOMER |
BRENDAi | 2.2.1.6, 399 |
SABIO-RKi | P17597 |
Miscellaneous databases
EvolutionaryTracei | P17597 |
PROi | PR:P17597 |
Gene expression databases
ExpressionAtlasi | P17597, baseline and differential |
Genevisiblei | P17597, AT |
Family and domain databases
CDDi | cd02015, TPP_AHAS, 1 hit |
InterProi | View protein in InterPro IPR012846, Acetolactate_synth_lsu IPR039368, AHAS_TPP 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 |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF00205, TPP_enzyme_M, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00118, acolac_lg, 1 hit |
PROSITEi | View protein in PROSITE PS00187, TPP_ENZYMES, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ILVB_ARATH | |
Accessioni | P17597Primary (citable) accession number: P17597 Secondary accession number(s): A0A174 Q94B64 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1990 |
Last sequence update: | August 1, 1990 | |
Last modified: | December 2, 2020 | |
This is version 183 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Genetically modified food, Reference proteomeDocuments
- 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