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Entry version 126 (07 Oct 2020)
Sequence version 1 (29 Mar 2005)
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Protein

Deoxyribose-phosphate aldolase

Gene

deoC

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

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate (PubMed:11598300, PubMed:17905878, PubMed:6749498). Can also catalyze the double aldol condensation of three acetaldehyde molecules, leading to the formation of 2,4,6-trideoxyhexose (Ref. 5).4 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 describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.23 mM for 2-deoxy-D-ribose 5-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.5 for 2-deoxy-D-ribose 5-phosphate cleavage.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: 2-deoxy-D-ribose 1-phosphate degradation

    This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate.UniRule annotationCurated
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Deoxyribose-phosphate aldolase (deoC), Deoxyribose-phosphate aldolase (deoC)
    This subpathway is part of the pathway 2-deoxy-D-ribose 1-phosphate degradation, 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 acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate, the pathway 2-deoxy-D-ribose 1-phosphate degradation 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei102Proton donor/acceptorUniRule annotation1 Publication1
    Active sitei167Schiff-base intermediate with acetaldehydeUniRule annotation1 Publication1 Publication1
    Active sitei201Proton donor/acceptorUniRule annotation2 Publications1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionLyase
    LigandSchiff base

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:DEOXYRIBOSE-P-ALD-MONOMER
    MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.2.4, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0A6L0

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

    More...
    UniPathwayi
    UPA00002;UER00468

    <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:
    Deoxyribose-phosphate aldolaseUniRule annotationCurated (EC:4.1.2.4UniRule annotation3 Publications)
    Short name:
    DERA2 PublicationsUniRule annotation
    Alternative name(s):
    2-deoxy-D-ribose 5-phosphate aldolase1 PublicationUniRule annotationCurated
    PhosphodeoxyriboaldolaseUniRule annotationCurated
    Short name:
    DeoxyriboaldolaseUniRule annotationCurated
    <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:deoC1 PublicationUniRule annotation
    Synonyms:dra, thyR
    Ordered Locus Names:b4381, JW4344
    <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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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

    GO - Cellular componenti

    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>Mutagenesisi47C → A or S: 3-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi102D → E: 44-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi102D → L: 2000-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi102D → N: 1500-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi137K → L: 20-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi167K → L: 1000-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi167K → R: 20-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi201K → L: 1500-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi201K → R: 1000-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi259Y → F: 200-fold decrease in catalytic efficiency. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB04087, Open Form of 2'-Deoxy-Ribofuranose-5'-Phosphate

    <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_00000572961 – 259Deoxyribose-phosphate aldolaseAdd BLAST259

    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 residuei167N6-acetyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A6L0

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

    More...
    PaxDbi
    P0A6L0

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A6L0

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0A6L0

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P0A6L0

    <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

    Monomer and homodimer.

    2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4263350, 25 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P0A6L0, 8 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b4381

    <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

    1259
    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
    P0A6L0

    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
    P0A6L0

    <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

    <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 DeoC/FbaB aldolase family. DeoC type 2 subfamily.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0274, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_053595_3_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A6L0

    KEGG Orthology (KO)

    More...
    KOi
    K01619

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A6L0

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00959, DeoC, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.70, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00592, DeoC_type2, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013785, Aldolase_TIM
    IPR011343, DeoC
    IPR002915, DeoC/FbaB/LacD_aldolase
    IPR023649, DeoC_typeII

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10889, PTHR10889, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01791, DeoC, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001357, DeoC, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01133, DeoC, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00126, deoC, 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.

    P0A6L0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP
    60 70 80 90 100
    RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE
    110 120 130 140 150
    VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL
    160 170 180 190 200
    IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF
    210 220 230 240 250
    KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH

    GDGKSASSY
    Length:259
    Mass (Da):27,734
    Last modified:March 29, 2005 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iABA50C625195D494
    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 conflicti18T → N in CAA26974 (PubMed:6749498).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
    X03224 Genomic DNA Translation: CAA26974.1
    U14003 Genomic DNA Translation: AAA97277.1
    U00096 Genomic DNA Translation: AAC77334.1
    AP009048 Genomic DNA Translation: BAE78370.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A01102, ADECD

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418798.1, NC_000913.3
    WP_001298497.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC77334; AAC77334; b4381
    BAE78370; BAE78370; BAE78370

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    52075304
    948902

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW4344
    eco:b4381

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2304

    <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
    X03224 Genomic DNA Translation: CAA26974.1
    U14003 Genomic DNA Translation: AAA97277.1
    U00096 Genomic DNA Translation: AAC77334.1
    AP009048 Genomic DNA Translation: BAE78370.1
    PIRiA01102, ADECD
    RefSeqiNP_418798.1, NC_000913.3
    WP_001298497.1, NZ_LN832404.1

    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
    1JCJX-ray1.10A/B1-259[»]
    1JCLX-ray1.05A/B1-259[»]
    1KTNX-ray1.40A/B1-250[»]
    1P1XX-ray0.99A/B1-259[»]
    5EKYX-ray1.10A1-259[»]
    5EL1X-ray1.25A1-259[»]
    5EMUX-ray1.50A1-259[»]
    SMRiP0A6L0
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4263350, 25 interactors
    IntActiP0A6L0, 8 interactors
    STRINGi511145.b4381

    Chemistry databases

    DrugBankiDB04087, Open Form of 2'-Deoxy-Ribofuranose-5'-Phosphate

    PTM databases

    iPTMnetiP0A6L0

    2D gel databases

    SWISS-2DPAGEiP0A6L0

    Proteomic databases

    jPOSTiP0A6L0
    PaxDbiP0A6L0
    PRIDEiP0A6L0

    Genome annotation databases

    EnsemblBacteriaiAAC77334; AAC77334; b4381
    BAE78370; BAE78370; BAE78370
    GeneIDi52075304
    948902
    KEGGiecj:JW4344
    eco:b4381
    PATRICifig|1411691.4.peg.2304

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0217

    Phylogenomic databases

    eggNOGiCOG0274, Bacteria
    HOGENOMiCLU_053595_3_1_6
    InParanoidiP0A6L0
    KOiK01619
    PhylomeDBiP0A6L0

    Enzyme and pathway databases

    UniPathwayiUPA00002;UER00468
    BioCyciEcoCyc:DEOXYRIBOSE-P-ALD-MONOMER
    MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER
    BRENDAi4.1.2.4, 2026
    SABIO-RKiP0A6L0

    Miscellaneous databases

    EvolutionaryTraceiP0A6L0

    Protein Ontology

    More...
    PROi
    PR:P0A6L0

    Family and domain databases

    CDDicd00959, DeoC, 1 hit
    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_00592, DeoC_type2, 1 hit
    InterProiView protein in InterPro
    IPR013785, Aldolase_TIM
    IPR011343, DeoC
    IPR002915, DeoC/FbaB/LacD_aldolase
    IPR023649, DeoC_typeII
    PANTHERiPTHR10889, PTHR10889, 1 hit
    PfamiView protein in Pfam
    PF01791, DeoC, 1 hit
    PIRSFiPIRSF001357, DeoC, 1 hit
    SMARTiView protein in SMART
    SM01133, DeoC, 1 hit
    TIGRFAMsiTIGR00126, deoC, 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 nameiDEOC_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: P0A6L0
    Secondary accession number(s): P00882, Q2M5T6
    <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: March 29, 2005
    Last modified: October 7, 2020
    This is version 126 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
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