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Protein

Fructose-bisphosphate aldolase 2, chloroplastic

Gene

FBA2

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

Plays a key role in glycolysis and gluconeogenesis.By similarity

<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 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=35 µM for fructose-bisphosphate for the cleavage reaction1 Publication
  1. Vmax=13 µmol/min/mg enzyme with fructose-bisphosphate as substrate1 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. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (PGIC), Glucose-6-phosphate isomerase (MJB21.12), Glucose-6-phosphate isomerase (AXX17_At4g28500), Glucose-6-phosphate isomerase (PGI1 (At4g24620)), Glucose-6-phosphate isomerase (AXX17_At5g40630), Glucose-6-phosphate isomerase, cytosolic (PGIC), Glucose-6-phosphate isomerase 1, chloroplastic (PGI1)
  3. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP-BETA), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP-BETA), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), 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 alpha (PFP-ALPHA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (PFP-ALPHA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 (PFP-BETA2), ATP-dependent 6-phosphofructokinase 3 (PFK3), ATP-dependent 6-phosphofructokinase 6 (PFK6), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 (PFP-BETA1), ATP-dependent 6-phosphofructokinase 7 (PFK7), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 1 (PFP-ALPHA1), ATP-dependent 6-phosphofructokinase 2 (PFK2), ATP-dependent 6-phosphofructokinase 4, chloroplastic (PFK4), ATP-dependent 6-phosphofructokinase 5, chloroplastic (PFK5), ATP-dependent 6-phosphofructokinase 1 (PFK1), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 2 (PFP-ALPHA2)
  4. Fructose-bisphosphate aldolase (AXX17_At2g16800), Fructose-bisphosphate aldolase (FBA4), Fructose-bisphosphate aldolase (FBA6), Fructose-bisphosphate aldolase (FBA7), Fructose-bisphosphate aldolase (AXX17_At3g47340), Fructose-bisphosphate aldolase (AXX17_At3g47340), Fructose-bisphosphate aldolase (At2g21330), Fructose-bisphosphate aldolase (AXX17_At4g30600), Fructose-bisphosphate aldolase (FBA1), Fructose-bisphosphate aldolase (AXX17_At4g44320), Fructose-bisphosphate aldolase (AXX17_At5g03010), Fructose-bisphosphate aldolase (FBA2), Fructose-bisphosphate aldolase (AXX17_At2g00100), Fructose-bisphosphate aldolase (FBA1), Fructose-bisphosphate aldolase (AXX17_At5g03010), Fructose-bisphosphate aldolase (FBA7), Fructose-bisphosphate aldolase (AXX17_At5g03010), Fructose-bisphosphate aldolase (AXX17_At2g33200), Fructose-bisphosphate aldolase (AXX17_At4g30610), Fructose-bisphosphate aldolase 7, cytosolic (FBA7), Fructose-bisphosphate aldolase 6, cytosolic (FBA6), Fructose-bisphosphate aldolase 2, chloroplastic (FBA2), Fructose-bisphosphate aldolase 3, chloroplastic (FBA3), Fructose-bisphosphate aldolase 5, cytosolic (FBA5), Fructose-bisphosphate aldolase 4, cytosolic (FBA4), Fructose-bisphosphate aldolase 1, chloroplastic (FBA1), Fructose-bisphosphate aldolase 8, cytosolic (FBA8)
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 ‘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 sitei95SubstrateBy similarity1
Binding sitei185SubstrateBy similarity1
<p>This subsection of the ‘Function’ 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 sitei225Proton acceptorBy similarity1
Active sitei267Schiff-base intermediate with dihydroxyacetone-PBy 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>Sitei398Necessary 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

  • fructose-bisphosphate aldolase activity Source: UniProtKB

GO - Biological processi

  • gluconeogenesis Source: UniProtKB
  • glycolytic process Source: UniProtKB
  • response to abscisic acid Source: TAIR
  • response to cadmium ion Source: TAIR

<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
LigandSchiff base

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT4G38970-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 2, chloroplasticCurated (EC:4.1.2.13Curated)
Short name:
AtFBA21 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:FBA21 Publication
Ordered Locus Names:At4g38970
ORF Names:F19H22.70
<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 4

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT4G38970

The Arabidopsis Information Resource

More...
TAIRi
locus:2120192 AT4G38970

<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; 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 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

Reduced growth rate. Unability to accumulate starch in leaves during daylight.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>Mutagenesisi394K → A: Loss of methylation, but no effect on enzyme activity. 1 Publication1

<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 – 46ChloroplastSequence analysisAdd BLAST46
<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_000028652747 – 398Fructose-bisphosphate aldolase 2, chloroplasticAdd BLAST352

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 residuei157PhosphoserineCombined sources1
Modified residuei215PhosphoserineCombined sources1
Modified residuei394N6,N6,N6-trimethyllysine1 Publication1

<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

Can be trimethylated at Lys-394 by LSMT-L. The methylation level has no influence on the ologomerization state or on the kinetic properties of the enzyme.1 Publication
Phosphorylated on tyrosine residues in response to abscisic acid (ABA) in germinating seeds.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q944G9

PRoteomics IDEntifications database

More...
PRIDEi
Q944G9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q944G9

<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

Highly expressed in rosettes leaves.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 and sucrose (PubMed:22561114). Induced by drought stress (PubMed:22561114).1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q944G9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q944G9 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

Homotetramer.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
15332, 3 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT4G38970.1

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q944G9

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

More...
SMRi
Q944G9

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Regioni309 – 311Substrate 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

Keywords - Domaini

Transit peptide

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
Q944G9

KEGG Orthology (KO)

More...
KOi
K01623

Identification of Orthologs from Complete Genome Data

More...
OMAi
KYTGDGE

Database of Orthologous Groups

More...
OrthoDBi
EOG09360CPA

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>.<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.

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

Isoform 1 (identifier: Q944G9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MASTSLLKAS PVLDKSEWVK GQSVLFRQPS SASVVLRNRA TSLTVRAASS
60 70 80 90 100
YADELVKTAK TIASPGRGIL AMDESNATCG KRLDSIGLEN TEANRQAFRT
110 120 130 140 150
LLVSAPGLGQ YVSGAILFEE TLYQSTTEGK KMVDVLVEQN IVPGIKVDKG
160 170 180 190 200
LVPLVGSNNE SWCQGLDGLS SRTAAYYQQG ARFAKWRTVV SIPNGPSALA
210 220 230 240 250
VKEAAWGLAR YAAISQDSGL VPIVEPEILL DGEHDIDRTY DVAEKVWAEV
260 270 280 290 300
FFYLAQNNVM FEGILLKPSM VTPGAESKDR ATPEQVAAYT LKLLRNRVPP
310 320 330 340 350
AVPGIMFLSG GQSEVEATLN LNAMNQAPNP WHVSFSYARA LQNTCLKTWG
360 370 380 390
GRPENVNAAQ TTLLARAKAN SLAQLGKYTG EGESEEAKEG MFVKGYTY
Length:398
Mass (Da):42,988
Last modified:July 27, 2011 - v2
<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:iE306F39ED18BD71D
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
F4JUJ5F4JUJ5_ARATH
Fructose-bisphosphate aldolase
FBA2 AtFBA2, At4g38970, F19H22.70, F19H22_70
381Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAB38817 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB80560 differs from that shown. Reason: Erroneous gene model prediction.Curated

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 conflicti163C → G in AAL16224 (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

More...
DDBJi
Links Updated
AL035679 Genomic DNA Translation: CAB38817.1 Sequence problems.
AL161594 Genomic DNA Translation: CAB80560.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE87002.1
AF428455 mRNA Translation: AAL16224.1
BT015870 mRNA Translation: AAU94433.1
AK226247 mRNA Translation: BAE98409.1

Protein sequence database of the Protein Information Resource

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PIRi
T06057

NCBI Reference Sequences

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RefSeqi
NP_568049.1, NM_120057.4 [Q944G9-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
At.21716
At.24925
At.72607
At.75329

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT4G38970.1; AT4G38970.1; AT4G38970 [Q944G9-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
830052

Gramene; a comparative resource for plants

More...
Gramenei
AT4G38970.1; AT4G38970.1; AT4G38970 [Q944G9-1]

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT4G38970

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
AL035679 Genomic DNA Translation: CAB38817.1 Sequence problems.
AL161594 Genomic DNA Translation: CAB80560.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE87002.1
AF428455 mRNA Translation: AAL16224.1
BT015870 mRNA Translation: AAU94433.1
AK226247 mRNA Translation: BAE98409.1
PIRiT06057
RefSeqiNP_568049.1, NM_120057.4 [Q944G9-1]
UniGeneiAt.21716
At.24925
At.72607
At.75329

3D structure databases

ProteinModelPortaliQ944G9
SMRiQ944G9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15332, 3 interactors
STRINGi3702.AT4G38970.1

PTM databases

iPTMnetiQ944G9

Proteomic databases

PaxDbiQ944G9
PRIDEiQ944G9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G38970.1; AT4G38970.1; AT4G38970 [Q944G9-1]
GeneIDi830052
GrameneiAT4G38970.1; AT4G38970.1; AT4G38970 [Q944G9-1]
KEGGiath:AT4G38970

Organism-specific databases

AraportiAT4G38970
TAIRilocus:2120192 AT4G38970

Phylogenomic databases

eggNOGiKOG1557 Eukaryota
COG3588 LUCA
HOGENOMiHOG000220876
InParanoidiQ944G9
KOiK01623
OMAiKYTGDGE
OrthoDBiEOG09360CPA

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00183

BioCyciARA:AT4G38970-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q944G9

Gene expression databases

ExpressionAtlasiQ944G9 baseline and differential
GenevisibleiQ944G9 AT

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...

<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 nameiALFP2_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: Q944G9
Secondary accession number(s): Q5XEU6, Q9SVJ6
<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: May 15, 2007
Last sequence update: July 27, 2011
Last modified: December 5, 2018
This is version 113 of the entry and version 2 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
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