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Protein

Fructose-bisphosphate aldolase A

Gene

ALDOA

Organism
Oryctolagus cuniculus (Rabbit)
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. In addition, may also function as scaffolding protein.1 Publication

Miscellaneous

In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.
Alkylation of Arg-43 inactivates the enzyme.

<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 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.
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 (GPI), Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM)
  4. Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase B (ALDOB)
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 sitei43SubstrateCombined sources1 Publication1
<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>Sitei73Essential for substrate cleavage1
Sitei108Essential for substrate cleavage1
Sitei147Alkylation inactivates the enzyme1
<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 sitei188Proton acceptor1 Publication1
Active sitei230Schiff-base intermediate with dihydroxyacetone-P1 Publication1
Binding sitei304SubstrateCombined sources1 Publication1
Sitei362Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base1
Sitei364Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate1

<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

  • glycolytic process Source: UniProtKB
  • negative regulation of Arp2/3 complex-mediated actin nucleation Source: CAFA
  • positive regulation of cell migration Source: CAFA
  • protein homotetramerization Source: UniProtKB

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.2.13 1749

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00883

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

More...
UniPathwayi
UPA00109;UER00183

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P00883

<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 A (EC:4.1.2.13)
Alternative name(s):
Muscle-type aldolase
<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:ALDOA
<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>OrganismiOryctolagus cuniculus (Rabbit)
<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 identifieri9986 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<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
  • UP000001811 <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 6

<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

Keywords - Cellular componenti

Cytoplasm

<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

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>Mutagenesisi35E → A: Reduces activity 14-fold. 1 Publication1
Mutagenesisi43R → A: Reduces activity 14-fold. 1 Publication1
Mutagenesisi129D → V: Alters protein-protein interactions, leading to a dimeric protein. 1
Mutagenesisi147K → A: Loss of activity. 1 Publication1
Mutagenesisi188E → A: Reduces activity over 100-fold. 1 Publication1
Mutagenesisi188E → Q: Reduces activity over 1000-fold. 1 Publication1
Mutagenesisi190E → Q: Reduces activity 20-fold. 1 Publication1
Mutagenesisi230K → M: Loss of activity. 1 Publication1
Mutagenesisi304R → A: Reduces activity 400-fold. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4695

<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 methionineiRemoved2 Publications
<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_00002169382 – 364Fructose-bisphosphate aldolase AAdd BLAST363

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 residuei9PhosphothreonineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei39PhosphoserineBy similarity1
Modified residuei42N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei46PhosphoserineBy similarity1
Modified residuei108N6-acetyllysineBy similarity1
Modified residuei111N6-acetyllysine; alternateBy similarity1
Modified residuei111N6-malonyllysine; alternateBy similarity1
Modified residuei132PhosphoserineBy similarity1
Modified residuei272PhosphoserineBy similarity1
Modified residuei312N6-malonyllysineBy similarity1
Modified residuei330N6-acetyllysineBy similarity1
Modified residuei361Deamidated asparagine; in form beta1 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

Asn-361 in form alpha is deaminated to Asp in form beta.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P00883

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00883

<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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSOCUG00000006329 Expressed in 3 organ(s), highest expression level in prefrontal cortex

<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. Interacts with SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+.6 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
1172078, 2 interactors

Protein interaction database and analysis system

More...
IntActi
P00883, 1 interactor

Molecular INTeraction database

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MINTi
P00883

STRING: functional protein association networks

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STRINGi
9986.ENSOCUP00000020204

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00883

<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

1364
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00883

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

More...
SMRi
P00883

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00883

<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>Regioni272 – 274Substrate bindingCombined sources1 Publication3

<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

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000010235

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220876

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG002386

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00883

KEGG Orthology (KO)

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KOi
K01623

Identification of Orthologs from Complete Genome Data

More...
OMAi
DYREMLF

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0A9T

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

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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>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.

P00883-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE
60 70 80 90 100
NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS
110 120 130 140 150
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKYSHEEIA
260 270 280 290 300
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
310 320 330 340 350
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG
360
AAASESLFIS NHAY
Length:364
Mass (Da):39,343
Last modified:January 23, 2007 - 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:iE61BCBC60F668324
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 conflicti35E → Q AA sequence (PubMed:1122141).Curated1
Sequence conflicti274 – 276GQS → SQE AA sequence (PubMed:1122142).Curated3
Sequence conflicti276S → E AA sequence (PubMed:1122142).Curated1
Sequence conflicti294 – 296KPW → WPK AA sequence (PubMed:1122142).Curated3
Sequence conflicti354S → R in CAA24246 (PubMed:6687628).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K02300 mRNA Translation: AAA31156.1
V00876 mRNA Translation: CAA24245.1
V00877 mRNA Translation: CAA24246.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A92444 ADRBA

NCBI Reference Sequences

More...
RefSeqi
NP_001075707.1, NM_001082238.1
XP_008256151.1, XM_008257929.2
XP_008256152.1, XM_008257930.2
XP_017197924.1, XM_017342435.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Ocu.864

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100009055

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100009055

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02300 mRNA Translation: AAA31156.1
V00876 mRNA Translation: CAA24245.1
V00877 mRNA Translation: CAA24246.1
PIRiA92444 ADRBA
RefSeqiNP_001075707.1, NM_001082238.1
XP_008256151.1, XM_008257929.2
XP_008256152.1, XM_008257930.2
XP_017197924.1, XM_017342435.1
UniGeneiOcu.864

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ADOX-ray1.90A/B/C/D2-364[»]
1EWDX-ray2.46A/B/C/D2-364[»]
1EWEX-ray2.60A/B/C/D2-364[»]
1EX5X-ray2.20A/B/C/D2-364[»]
1J4EX-ray2.65A/B/C/D2-364[»]
1ZAHX-ray1.80A/B/C/D2-364[»]
1ZAIX-ray1.76A/B/C/D2-364[»]
1ZAJX-ray1.89A/B/C/D2-364[»]
1ZALX-ray1.89A/B/C/D2-364[»]
2OT0X-ray2.05A/B/C/D2-364[»]
2OT1X-ray2.05A/B/C/D2-364[»]
2QUTX-ray1.88A/B/C/D2-364[»]
2QUUX-ray1.98A/B/C/D2-364[»]
2QUVX-ray2.22A/B/C/D2-364[»]
3B8DX-ray2.00A/B/C/D2-364[»]
3BV4X-ray1.70A5-344[»]
3DFNX-ray1.86A/B/C/D2-364[»]
3DFOX-ray1.94A/B/C/D2-364[»]
3DFPX-ray2.05A/B/C/D2-364[»]
3DFQX-ray1.82A/B/C/D2-364[»]
3DFSX-ray2.03A/B/C/D2-364[»]
3DFTX-ray1.94A/B/C/D2-364[»]
3LGEX-ray2.20A/B/C/D2-364[»]
3TU9X-ray2.09A/B/C/D2-364[»]
5F4XX-ray1.84A/B/C/D2-364[»]
5TLEX-ray1.58A/B/C/D2-364[»]
5TLHX-ray2.20A/B/C/D2-364[»]
5TLWX-ray2.29A/B/C/D2-364[»]
5TLZX-ray1.97A/B/C/D2-364[»]
5VY5electron microscopy2.60A/B/C/D2-364[»]
6ALDX-ray2.30A/B/C/D2-364[»]
ProteinModelPortaliP00883
SMRiP00883
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1172078, 2 interactors
IntActiP00883, 1 interactor
MINTiP00883
STRINGi9986.ENSOCUP00000020204

Chemistry databases

BindingDBiP00883
ChEMBLiCHEMBL4695

Protein family/group databases

MoonProtiP00883

PTM databases

iPTMnetiP00883

Proteomic databases

PRIDEiP00883

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329
GeneIDi100009055
KEGGiocu:100009055

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
226

Phylogenomic databases

eggNOGiKOG1557 Eukaryota
COG3588 LUCA
GeneTreeiENSGT00390000010235
HOGENOMiHOG000220876
HOVERGENiHBG002386
InParanoidiP00883
KOiK01623
OMAiDYREMLF
OrthoDBiEOG091G0A9T

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00183

BRENDAi4.1.2.13 1749
SABIO-RKiP00883

Miscellaneous databases

EvolutionaryTraceiP00883

Protein Ontology

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PROi
PR:P00883

Gene expression databases

BgeeiENSOCUG00000006329 Expressed in 3 organ(s), highest expression level in prefrontal cortex

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

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ProtoNeti
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<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 nameiALDOA_RABIT
<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: P00883
Secondary accession number(s): Q28671
<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: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 163 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 programChordata 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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