Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 151 (16 Oct 2019)
Sequence version 1 (01 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Fructose-bisphosphate aldolase 6, cytosolic

Gene

FBA6

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

Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis (PubMed:21782461). Associates with GAPC1 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress (PubMed:23316205).2 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Total and irreversible inhibition by S-nitrosoglutathione (GSNO) (PubMed:21782461). Partial and reversible inhibition by oxidized glutathione (GSSG) (PubMed:21782461).1 Publication

<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>Kineticsi

  1. KM=25 µM for fructose 1,6-bisphosphate1 Publication

    <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: glycolysis

    This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.Curated
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Phosphotransferase (AXX17_At4g33470), Hexokinase-4 (At3g20040), Hexokinase-1 (HXK1), Phosphotransferase (AXX17_At3g21380), Phosphotransferase (AXX17_At1g41900), Phosphotransferase (AXX17_At2g15190), Phosphotransferase (HKL1), Phosphotransferase (AXX17_At1g44660), Phosphotransferase (AXX17_At1g41910), Hexokinase-2 (HXK2), Phosphotransferase (AXX17_At4g43120), Phosphotransferase (HKL1), Phosphotransferase (HXK3), Hexokinase-like 1 protein (At1g47840), Hexokinase-3 (At1g50460), Phosphotransferase (At4g29130), Phosphotransferase (HXK2), Phosphotransferase (At1g47845), Probable hexokinase-like 2 protein (At4g37840)
    2. Glucose-6-phosphate isomerase (AXX17_At4g28500), Glucose-6-phosphate isomerase (MJB21.12), Glucose-6-phosphate isomerase (PGI1 (At4g24620)), Glucose-6-phosphate isomerase, cytosolic (PGIC), Glucose-6-phosphate isomerase (PGIC), Glucose-6-phosphate isomerase 1, chloroplastic (PGI1), Glucose-6-phosphate isomerase (AXX17_At5g40630)
    3. ATP-dependent 6-phosphofructokinase 1 (PFK1), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase 5, chloroplastic (PFK5), ATP-dependent 6-phosphofructokinase 4, chloroplastic (PFK4), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP-BETA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (PFP-ALPHA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (PFP-ALPHA), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase 2 (PFK2), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP-BETA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 1 (PFP-ALPHA1), ATP-dependent 6-phosphofructokinase 6 (PFK6), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 (PFP-BETA1), ATP-dependent 6-phosphofructokinase 7 (PFK7), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 (PFP-BETA2), ATP-dependent 6-phosphofructokinase 3 (PFK3), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 2 (PFP-ALPHA2), ATP-dependent 6-phosphofructokinase (PFK)
    4. Fructose-bisphosphate aldolase 5, cytosolic (FBA5), Fructose-bisphosphate aldolase (FBA6), Fructose-bisphosphate aldolase (AXX17_At3g47340), Fructose-bisphosphate aldolase (FBA1), Fructose-bisphosphate aldolase (FBA1), Fructose-bisphosphate aldolase (FBA4), Fructose-bisphosphate aldolase (AXX17_At2g16800), Fructose-bisphosphate aldolase (AXX17_At4g44320), Fructose-bisphosphate aldolase (AXX17_At5g03010), Fructose-bisphosphate aldolase (AXX17_At4g30610), Fructose-bisphosphate aldolase (FBA2), Fructose-bisphosphate aldolase 1, chloroplastic (FBA1), Fructose-bisphosphate aldolase (AXX17_At5g03010), Fructose-bisphosphate aldolase 8, cytosolic (FBA8), Fructose-bisphosphate aldolase 7, cytosolic (FBA7), Fructose-bisphosphate aldolase 3, chloroplastic (FBA3), Fructose-bisphosphate aldolase 6, cytosolic (FBA6), Fructose-bisphosphate aldolase (FBA7), Fructose-bisphosphate aldolase (AXX17_At2g00100), Fructose-bisphosphate aldolase (FBA7), Fructose-bisphosphate aldolase (AXX17_At4g30600), Fructose-bisphosphate aldolase 2, chloroplastic (FBA2), Fructose-bisphosphate aldolase (At2g21330), Fructose-bisphosphate aldolase (AXX17_At3g47340), Fructose-bisphosphate aldolase (AXX17_At5g03010), Fructose-bisphosphate aldolase (AXX17_At2g33200), Fructose-bisphosphate aldolase 4, cytosolic (FBA4)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei39SubstrateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei183Proton acceptorBy similarity1
    Active sitei225Schiff-base intermediate with dihydroxyacetone-PBy similarity1
    Binding sitei298SubstrateBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei358Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity1

    <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 functionLyase
    Biological processGlycolysis, Stress response
    LigandSchiff base

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    ARA:AT2G36460-MONOMER

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

    More...
    UniPathwayi
    UPA00109;UER00183

    <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:
    Fructose-bisphosphate aldolase 6, cytosolicCurated (EC:4.1.2.131 Publication)
    Short name:
    AtFBA61 Publication
    Alternative name(s):
    Cytosolic aldolase 21 Publication
    Short name:
    cAld21 Publication
    <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:FBA61 Publication
    Ordered Locus Names:At2g36460Imported
    <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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    <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 2

    Organism-specific databases

    Arabidopsis Information Portal

    More...
    Araporti
    AT2G36460

    The Arabidopsis Information Resource

    More...
    TAIRi
    locus:2044856 AT2G36460

    <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

    Cytoplasm, Mitochondrion, Nucleus

    <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 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

    No visible phenotype under normal growth conditions, but mutant seeds have increased germination rate in presence of high salt or high mannitol, and decreased germination rate in presence of abscisic acid (ABA), glucose, fructose and sucrose.1 Publication

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
    <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_00004372402 – 358Fructose-bisphosphate aldolase 6, cytosolicAdd BLAST357

    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 residuei2N-acetylserineBy similarity1
    Modified residuei68S-glutathionyl cysteine; transient1 Publication1
    Modified residuei173S-glutathionyl cysteine; transient; alternate1 Publication1
    Modified residuei173S-nitrosocysteine; transient; alternate1 Publication1
    Modified residuei350PhosphoserineBy similarity1
    Modified residuei354N6,N6,N6-trimethyllysineBy similarity1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    S-glutathionylated at Cys-68 and Cys-173.1 Publication
    S-nitrosylated at Cys-173.1 Publication

    Keywords - PTMi

    Acetylation, Glutathionylation, Methylation, Phosphoprotein, S-nitrosylation

    Proteomic databases

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

    More...
    PaxDbi
    Q9SJQ9

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9SJQ9

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9SJQ9

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q9SJQ9

    <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

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in roots, rosettes leaves, cauline leaves, stems and flowers.1 Publication

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By glucose, fructose and sucrose (PubMed:22561114). Induced by abiotic stresses (PubMed:22561114). Induced by cadmium (PubMed:16502469).2 Publications

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9SJQ9 baseline and differential

    <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

    Homotetramer (By similarity).

    Interacts with TRX1 and TRX3 (PubMed:21782461).

    Interacts with GAPC1 AND VDAC3 (PubMed:23316205).

    By similarity2 Publications

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    Q9SJQ9, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    3702.AT2G36460.1

    <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

    3D structure databases

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

    More...
    SMRi
    Q9SJQ9

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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>Regioni266 – 268Substrate bindingBy similarity3

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1557 Eukaryota
    COG3588 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000220876

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9SJQ9

    KEGG Orthology (KO)

    More...
    KOi
    K01623

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QATLGTY

    Database of Orthologous Groups

    More...
    OrthoDBi
    799973at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9SJQ9

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.70, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029768 Aldolase_I_AS
    IPR013785 Aldolase_TIM
    IPR000741 FBA_I

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00274 Glycolytic, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00158 ALDOLASE_CLASS_I, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <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.

    This entry describes 1 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoform i produced by alternative splicing. AlignAdd to basket
    Note: A number of isoforms are produced. According to EST sequences.Curated

    This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q9SJQ9-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MSSFTSKFAD ELIANAAYIG TPGKGILAAD ESTGTIGKRL ASINVENVES
    60 70 80 90 100
    NRRALRELLF TTPGALPCLS GVILFEETLY QKSSDGTPFV DMLKSAGVLP
    110 120 130 140 150
    GIKVDKGTVE LAGTNGETTT QGLDGLGDRC KKYYEAGARF AKWRAVLKIG
    160 170 180 190 200
    VNEPSQLAIH ENAYGLARYA VICQENGLVP IVEPEILVDG SHDIQKCAAV
    210 220 230 240 250
    TERVLAACYK ALSDHHVLLE GTLLKPNMVT PGSESAKVAP EVIAEHTVRA
    260 270 280 290 300
    LQRTVPAAVP AIVFLSGGQS EEEATRNLNA MNQLKTKKPW SLSFSFGRAL
    310 320 330 340 350
    QQSTLKTWGG KEENVKKAQE AFLVRCKANS EATLGAYKGD AKLGEGAAES

    LHVKDYKY
    Length:358
    Mass (Da):38,387
    Last modified:May 1, 2000 - 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:i0426179B1F27B5A6
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    B3H6D7B3H6D7_ARATH
    Fructose-bisphosphate aldolase
    FBA6 At2g36460, F1O11.9, F1O11_9
    267Annotation score:

    Annotation score:2 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>

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AC006919 Genomic DNA Translation: AAD24630.1
    CP002685 Genomic DNA Translation: AEC09256.1
    AY034897 mRNA Translation: AAK59404.1
    AY063044 mRNA Translation: AAL34218.1
    AK226842 mRNA Translation: BAE98935.1
    AY085114 mRNA Translation: AAM61668.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A84781

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_181187.1, NM_129203.3 [Q9SJQ9-1]

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    AT2G36460.1; AT2G36460.1; AT2G36460 [Q9SJQ9-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    818220

    Gramene; a comparative resource for plants

    More...
    Gramenei
    AT2G36460.1; AT2G36460.1; AT2G36460 [Q9SJQ9-1]

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ath:AT2G36460

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    AC006919 Genomic DNA Translation: AAD24630.1
    CP002685 Genomic DNA Translation: AEC09256.1
    AY034897 mRNA Translation: AAK59404.1
    AY063044 mRNA Translation: AAL34218.1
    AK226842 mRNA Translation: BAE98935.1
    AY085114 mRNA Translation: AAM61668.1
    PIRiA84781
    RefSeqiNP_181187.1, NM_129203.3 [Q9SJQ9-1]

    3D structure databases

    SMRiQ9SJQ9
    ModBaseiSearch...

    Protein-protein interaction databases

    IntActiQ9SJQ9, 1 interactor
    STRINGi3702.AT2G36460.1

    PTM databases

    iPTMnetiQ9SJQ9
    SwissPalmiQ9SJQ9

    Proteomic databases

    PaxDbiQ9SJQ9
    PRIDEiQ9SJQ9

    Genome annotation databases

    EnsemblPlantsiAT2G36460.1; AT2G36460.1; AT2G36460 [Q9SJQ9-1]
    GeneIDi818220
    GrameneiAT2G36460.1; AT2G36460.1; AT2G36460 [Q9SJQ9-1]
    KEGGiath:AT2G36460

    Organism-specific databases

    AraportiAT2G36460
    TAIRilocus:2044856 AT2G36460

    Phylogenomic databases

    eggNOGiKOG1557 Eukaryota
    COG3588 LUCA
    HOGENOMiHOG000220876
    InParanoidiQ9SJQ9
    KOiK01623
    OMAiQATLGTY
    OrthoDBi799973at2759
    PhylomeDBiQ9SJQ9

    Enzyme and pathway databases

    UniPathwayiUPA00109;UER00183
    BioCyciARA:AT2G36460-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q9SJQ9

    Gene expression databases

    ExpressionAtlasiQ9SJQ9 baseline and differential

    Family and domain databases

    Gene3Di3.20.20.70, 1 hit
    InterProiView protein in InterPro
    IPR029768 Aldolase_I_AS
    IPR013785 Aldolase_TIM
    IPR000741 FBA_I
    PfamiView protein in Pfam
    PF00274 Glycolytic, 1 hit
    PROSITEiView protein in PROSITE
    PS00158 ALDOLASE_CLASS_I, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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 nameiALFC6_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: Q9SJQ9
    <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: October 5, 2016
    Last sequence update: May 1, 2000
    Last modified: October 16, 2019
    This is version 151 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again