Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P08203 (ARAD_ECOLI)

Entry version 179 (07 Apr 2021)
Sequence version 2 (01 Aug 1991)
Previous versions | rss
Add a publicationFeedback
Protein

L-ribulose-5-phosphate 4-epimerase AraD

Gene

araD

Organism
Escherichia coli (strain K12)
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

Involved in the degradation of L-arabinose (PubMed:13890280). Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction).UniRule annotation6 Publications

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

Zn2+UniRule annotation4 PublicationsNote: Binds 1 zinc ion per subunit (PubMed:9548961, PubMed:10769139, PubMed:11732895, PubMed:11732896). Also able to use cobalt and manganese ions, but less efficiently (PubMed:10769139).UniRule annotation4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by glycolohydroxamate at concentration above 0.1 mM.1 Publication

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

Kcat is 20.4 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:9548961). Kcat is 19.4 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:11732896). Kcat is 17.3 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:10769139). Kcat is 10.6 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (at pH 7) (PubMed:10769138). Kcat is 4.23 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (at pH 5.5) (PubMed:10769138).4 Publications
  1. KM=0.17 µM for Zn2+1 Publication
  2. KM=0.29 µM for Co2+1 Publication
  3. KM=0.54 µM for Mn2+1 Publication
  4. KM=47 µM for L-ribulose 5-phosphate (LRu5P) (with zinc ion)2 Publications
  5. KM=87 µM for L-ribulose 5-phosphate (LRu5P) (with zinc ion)1 Publication
  6. KM=95 µM for L-ribulose 5-phosphate (LRu5P) (with zinc ion)1 Publication
  7. KM=110 µM for L-ribulose 5-phosphate (LRu5P) (with cobalt ion)1 Publication
  8. KM=425 µM for L-ribulose 5-phosphate (LRu5P) (with manganese ion)1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    <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: L-arabinose degradation via L-ribulose

    This protein is involved in step 3 of the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (bacterial route).UniRule annotation1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. L-arabinose isomerase (araA), L-arabinose isomerase (araA)
    2. Ribulokinase (araB), Ribulokinase (araB)
    3. L-ribulose-5-phosphate 4-epimerase (araD), L-ribulose-5-phosphate 4-epimerase AraD (araD)
    This subpathway is part of the pathway L-arabinose degradation via L-ribulose, 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-xylulose 5-phosphate from L-arabinose (bacterial route), the pathway L-arabinose degradation via L-ribulose 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 indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi76ZincUniRule annotation2 Publications1
    Metal bindingi95Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications2 Publications1
    Metal bindingi97Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications2 Publications1
    <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 sitei120Proton donor/acceptorUniRule annotation1 Publication1
    Metal bindingi171Zinc; via tele nitrogenUniRule annotationCombined sources1 Publication2 Publications1
    Active sitei229Proton donor/acceptorUniRule annotation1 Publication1

    <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

    • aldehyde-lyase activity Source: GO_Central
    • L-ribulose-phosphate 4-epimerase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB
    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 functionIsomerase
    Biological processArabinose catabolism, Carbohydrate metabolism
    LigandCobalt, Manganese, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:RIBULPEPIM-MONOMER
    MetaCyc:RIBULPEPIM-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P08203

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

    More...    UniPathwayi    		UPA00145;UER00567

    <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:
    L-ribulose-5-phosphate 4-epimerase AraD1 PublicationUniRule annotation (EC:5.1.3.4UniRule annotation5 Publications)
    Alternative name(s):
    Phosphoribulose isomeraseUniRule annotation
    <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:araD1 PublicationUniRule annotation
    Ordered Locus Names:b0061, JW0060
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    <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

    <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

    Cells lacking this gene accumulate large amount of L-ribulose 5-phosphate when incubated with L-arabinose.1 Publication

    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>Mutagenesisi28N → A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P). 1 Publication1
    Mutagenesisi42K → M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P). 1 Publication1
    Mutagenesisi76D → N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected. 2 Publications1
    Mutagenesisi95H → N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). 2 Publications1
    Mutagenesisi97H → N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate. 2 Publications1
    Mutagenesisi116T → E or Y: Loss of the epimerase activity due to an increased steric bulk introduced by the mutation which causes a conformational change that is incompatible with catalysis. 1 Publication1
    Mutagenesisi120D → N: Loss of the epimerase activity. 1 Publication1
    Mutagenesisi142E → Q: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected. 1 Publication1
    Mutagenesisi218H → N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected. 1 Publication1
    Mutagenesisi229Y → F: Loss of the epimerase activity. 2 Publications1

    <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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001629191 – 231L-ribulose-5-phosphate 4-epimerase AraDAdd BLAST231

    Proteomic databases

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

    More...    PaxDbi    		P08203

    PRoteomics IDEntifications database

    More...    PRIDEi    		P08203

    <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 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

    Induced by arabinose. Transcription is dependent on the transcription factor AraC, the cAMP receptor protein (CRP) and cAMP (PubMed:328165, PubMed:2962192, PubMed:7768852). Also induced by L-lyxose (PubMed:10913097).4 Publications

    <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.

    UniRule annotation4 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4263043, 1 interactor

    Database of interacting proteins

    More...    DIPi    		DIP-9126N

    Protein interaction database and analysis system

    More...    IntActi    		P08203, 4 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0061

    <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

    1231
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...    SMRi    		P08203

    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    		P08203

    <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>Regioni27 – 28Substrate bindingUniRule annotationBy similarity2
    Regioni44 – 45Substrate bindingUniRule annotationBy similarity2
    Regioni74 – 75Substrate bindingUniRule annotationBy similarity2

    <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 aldolase class II family. AraD/FucA subfamily.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0235, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_006033_5_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P08203

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P08203

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.225.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00989, AraD_entero, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001303, Aldolase_II/adducin_N
    IPR036409, Aldolase_II/adducin_N_sf
    IPR004661, AraD
    IPR033748, AraD_entero

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00596, Aldolase_II, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM01007, Aldolase_II, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53639, SSF53639, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00760, araD, 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>Sequencei

    <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.

    P08203-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLEDLKRQVL EANLALPKHN LVTLTWGNVS AVDRERGVFV IKPSGVDYSV 
            60         70         80         90        100
    MTADDMVVVS IETGEVVEGT KKPSSDTPTH RLLYQAFPSI GGIVHTHSRH 
           110        120        130        140        150
    ATIWAQAGQS IPATGTTHAD YFYGTIPCTR KMTDAEINGE YEWETGNVIV 
           160        170        180        190        200
    ETFEKQGIDA AQMPGVLVHS HGPFAWGKNA EDAVHNAIVL EEVAYMGIFC 
           210        220        230 
    RQLAPQLPDM QQTLLDKHYL RKHGAKAYYG Q
    Length:231
    Mass (Da):25,519
    Last modified:August 1, 1991 - 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:i1753F75958332163
    GO

    <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 25522 Da. Determined by ESI. 1 Publication

    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
    		M15263 Genomic DNA Translation: AAA23464.1
    M35371 Genomic DNA No translation available.
    M62646 Genomic DNA Translation: AAA24405.1
    U00096 Genomic DNA Translation: AAC73172.1
    AP009048 Genomic DNA Translation: BAB96630.1
    M37727 Genomic DNA Translation: AAA23683.1
    M38283 Genomic DNA Translation: AAA63763.1
    X56048 Genomic DNA Translation: CAA39519.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		E64727, ISECP4

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414603.1, NC_000913.3
    WP_000888666.1, NZ_STEB01000010.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73172; AAC73172; b0061
    BAB96630; BAB96630; BAB96630

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		57730861
    945294

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0060
    eco:b0061

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2222

    <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
    		M15263 Genomic DNA Translation: AAA23464.1
    M35371 Genomic DNA No translation available.
    M62646 Genomic DNA Translation: AAA24405.1
    U00096 Genomic DNA Translation: AAC73172.1
    AP009048 Genomic DNA Translation: BAB96630.1
    M37727 Genomic DNA Translation: AAA23683.1
    M38283 Genomic DNA Translation: AAA63763.1
    X56048 Genomic DNA Translation: CAA39519.1
    PIRiE64727, ISECP4
    RefSeqiNP_414603.1, NC_000913.3
    WP_000888666.1, NZ_STEB01000010.1

    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
    1JDIX-ray2.40A/B/C/D/E/F1-231[»]
    1K0WX-ray2.10A/B/C/D/E/F1-231[»]
    SMRiP08203
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4263043, 1 interactor
    DIPiDIP-9126N
    IntActiP08203, 4 interactors
    STRINGi511145.b0061

    Proteomic databases

    PaxDbiP08203
    PRIDEiP08203

    Genome annotation databases

    EnsemblBacteriaiAAC73172; AAC73172; b0061
    BAB96630; BAB96630; BAB96630
    GeneIDi57730861
    945294
    KEGGiecj:JW0060
    eco:b0061
    PATRICifig|1411691.4.peg.2222

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB0053

    Phylogenomic databases

    eggNOGiCOG0235, Bacteria
    HOGENOMiCLU_006033_5_0_6
    InParanoidiP08203
    PhylomeDBiP08203

    Enzyme and pathway databases

    UniPathwayiUPA00145;UER00567
    BioCyciEcoCyc:RIBULPEPIM-MONOMER
    MetaCyc:RIBULPEPIM-MONOMER
    SABIO-RKiP08203

    Miscellaneous databases

    EvolutionaryTraceiP08203

    Protein Ontology

    More...    PROi    		PR:P08203

    Family and domain databases

    Gene3Di3.40.225.10, 1 hit
    HAMAPiMF_00989, AraD_entero, 1 hit
    InterProiView protein in InterPro
    IPR001303, Aldolase_II/adducin_N
    IPR036409, Aldolase_II/adducin_N_sf
    IPR004661, AraD
    IPR033748, AraD_entero
    PfamiView protein in Pfam
    PF00596, Aldolase_II, 1 hit
    SMARTiView protein in SMART
    SM01007, Aldolase_II, 1 hit
    SUPFAMiSSF53639, SSF53639, 1 hit
    TIGRFAMsiTIGR00760, araD, 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 nameiARAD_ECOLI
    <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: P08203
    <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: August 1, 1988
    Last sequence update: August 1, 1991
    Last modified: April 7, 2021
    This is version 179 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 programProkaryotic 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
    Main funding by: National Institutes of Health

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

    Do not show this banner again