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UniProtKB - P00883 (ALDOA_RABIT)

Entry version 175 (02 Dec 2020)
Sequence version 2 (23 Jan 2007)
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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%5Fsection">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%5Fsection">'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. Hexokinase (HK1), Hexokinase (HK2), Hexokinase (HKDC1), Hexokinase (HK3), Hexokinase (HK2), Hexokinase (HK1), Hexokinase (HK3), Hexokinase (HK2), Hexokinase (HK3)
  2. Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase (PFKM), PFK domain-containing protein, ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM)
  4. Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase
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%5Fsection">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 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 <a href="http://www.uniprot.org/help/function%5Fsection">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 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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%5Fand%5Fbiotech%5Fsection">'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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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 residuei99N6-(2-hydroxyisobutyryl)lysineBy 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%5Fprocessing%5Fsection">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, Hydroxylation, 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

MetOSite database of methionine sulfoxide sites

More...MetOSitei		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 smooth muscle tissue and 17 other tissues

<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%5Fsection">'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%5Fsection">'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

More...MINTi		P00883

STRING: functional protein association networks

More...STRINGi		9986.ENSOCUP00000008499

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

The Protein Circular Dichroism Data Bank

More...PCDDBi		P00883

Small Angle Scattering Biological Data Bank

More...SASBDBi		P00883

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

More...SMRi		P00883

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

Belongs to the class I fructose-bisphosphate aldolase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1557, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182987

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_031243_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00883

Identification of Orthologs from Complete Genome Data

More...OMAi		DYREMLF

Database of Orthologous Groups

More...OrthoDBi		799973at2759

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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

<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
A0A5F9D5U7A0A5F9D5U7_RABIT
Fructose-bisphosphate aldolase
419Annotation 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>

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

More...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

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%5Freferences%5Fsection">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

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[»]
6MWQelectron microscopy3.00A/B/C/D12-348[»]
6V20electron microscopy2.13A/B/C/D3-345[»]
PCDDBiP00883
SASBDBiP00883
SMRiP00883
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi1172078, 2 interactors
IntActiP00883, 1 interactor
MINTiP00883
STRINGi9986.ENSOCUP00000008499

Chemistry databases

BindingDBiP00883
ChEMBLiCHEMBL4695

Protein family/group databases

MoonProtiP00883

PTM databases

iPTMnetiP00883
MetOSiteiP00883

Proteomic databases

PRIDEiP00883

Genome annotation databases

EnsembliENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329
GeneIDi100009055
KEGGiocu:100009055

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		226

Phylogenomic databases

eggNOGiKOG1557, Eukaryota
GeneTreeiENSGT00950000182987
HOGENOMiCLU_031243_1_0_1
InParanoidiP00883
OMAiDYREMLF
OrthoDBi799973at2759

Enzyme and pathway databases

UniPathwayiUPA00109;UER00183
BRENDAi4.1.2.13, 1749
SABIO-RKiP00883

Miscellaneous databases

EvolutionaryTraceiP00883

Protein Ontology

More...PROi		PR:P00883

Gene expression databases

BgeeiENSOCUG00000006329, Expressed in smooth muscle tissue and 17 other tissues

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 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%5Fand%5Fisoforms">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 2, 2020
This is version 175 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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