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Entry version 173 (13 Feb 2019)
Sequence version 1 (01 Aug 1990)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 7.0-7.5.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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 (AXX17_At3g42690), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3), Branched-chain-amino-acid aminotransferase 6 (BCAT6)
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 (AXX17_At3g42690), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (AXX17_At3g53150), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3), Branched-chain-amino-acid aminotransferase 6 (BCAT6)
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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi331 – 332FAD1 Publication2
Nucleotide bindingi349 – 352FAD1 Publication4
Nucleotide bindingi371 – 375FAD1 Publication5
Nucleotide bindingi395 – 396FAD1 Publication2
Nucleotide bindingi414 – 415FAD1 Publication2
Nucleotide bindingi508 – 509FAD1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis, Herbicide resistance
LigandFAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT3G48560-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.2.1.6 399

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P17597

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00047;UER00055

UPA00049;UER00059

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ALS
Synonyms:AHAS, CSR1, TZP5
Ordered Locus Names:At3g48560
ORF Names:T8P19.70
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT3G48560

The Arabidopsis Information Resource

More...
TAIRi
locus:2114525 AT3G48560

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Introduced by genetic manipulation and expressed in sulfonylurea resistant plants.

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Lethal when homozygous.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4263

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 55ChloroplastSequence analysisAdd BLAST55
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003565556 – 670Acetolactate synthase, chloroplasticAdd BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei340Cysteine sulfinic acid (-SO2H)2 Publications1

Keywords - PTMi

Oxidation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P17597

PRoteomics IDEntifications database

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PRIDEi
P17597

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P17597 AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
9334, 1 interactor

Database of interacting proteins

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DIPi
DIP-61092N

STRING: functional protein association networks

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STRINGi
3702.AT3G48560.1

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P17597

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1670
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
5K2OX-ray2.87A86-667[»]
5K3SX-ray2.87A86-667[»]
5K6QX-ray2.95A86-667[»]
5K6RX-ray2.73A86-667[»]
5K6TX-ray2.76A86-667[»]
5WJ1X-ray2.52A86-667[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P17597

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P17597

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P17597

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili414 – 446Sequence analysisAdd BLAST33

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4166 Eukaryota
COG0028 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000258448

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P17597

KEGG Orthology (KO)

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KOi
K01652

Identification of Orthologs from Complete Genome Data

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OMAi
QGMVRQW

Database of Orthologous Groups

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OrthoDBi
1132247at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P17597

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02015 TPP_AHAS, 1 hit

Integrated resource of protein families, domains and functional sites

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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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00118 acolac_lg, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDA697A8DD155F160
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

Protein sequence database of the Protein Information Resource

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PIRi
S09502 YCMU

NCBI Reference Sequences

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RefSeqi
NP_190425.1, NM_114714.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
At.22295
At.72000

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT3G48560.1; AT3G48560.1; AT3G48560

Database of genes from NCBI RefSeq genomes

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GeneIDi
824015

Gramene; a comparative resource for plants

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Gramenei
AT3G48560.1; AT3G48560.1; AT3G48560

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ath:AT3G48560

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
5K2OX-ray2.87A86-667[»]
5K3SX-ray2.87A86-667[»]
5K6QX-ray2.95A86-667[»]
5K6RX-ray2.73A86-667[»]
5K6TX-ray2.76A86-667[»]
5WJ1X-ray2.52A86-667[»]
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

AraportiAT3G48560
TAIRilocus:2114525 AT3G48560

Phylogenomic databases

eggNOGiKOG4166 Eukaryota
COG0028 LUCA
HOGENOMiHOG000258448
InParanoidiP17597
KOiK01652
OMAiQGMVRQW
OrthoDBi1132247at2759
PhylomeDBiP17597

Enzyme and pathway databases

UniPathwayi
UPA00047;UER00055

UPA00049;UER00059

BioCyciARA:AT3G48560-MONOMER
BRENDAi2.2.1.6 399
SABIO-RKiP17597

Miscellaneous databases

EvolutionaryTraceiP17597

Protein Ontology

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PROi
PR:P17597

Gene expression databases

GenevisibleiP17597 AT

Family and domain databases

CDDicd02015 TPP_AHAS, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits
TIGRFAMsiTIGR00118 acolac_lg, 1 hit
PROSITEiView protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiILVB_ARATH
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P17597
Secondary accession number(s): A0A174
, Q5FV34, Q8L7Y7, Q94B64
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 13, 2019
This is version 173 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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