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Entry version 170 (17 Jun 2020)
Sequence version 1 (01 Apr 1988)
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Protein

Pyruvate dehydrogenase [ubiquinone]

Gene

poxB

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

A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO2. It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone (By similarity) (PubMed:18988747, PubMed:2663858, PubMed:365232). The main pathway for acetate production during stationary phase (PubMed:16080684).UniRule annotation4 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

Protein has several cofactor binding sites:

<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

The C-terminus inhibits activity; it has to move for the enzyme to be active (PubMed:18988747). Activated by lipid-binding, which occurs via the C-terminus; detergents also activate the enzyme (PubMed:334770, PubMed:334771, PubMed:2663858, PubMed:18988747). Specifically activated by palmitic acid; 12 (lauric) and 14-carbon (myristic) fatty acids as well as unsaturated 16 and 18-carbon fatty acids also activate the enzyme (PubMed:6385860). Lipid affinity is increased in the presence of pyruvate plus the thiamine pyrophosphate cofactor (PubMed:334770, PubMed:334771, PubMed:2663858, PubMed:18988747).UniRule annotation5 Publications

<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 7 sec(-1) for non-activated, 200 sec(-1) for activated form.1 Publication
  1. KM=90 mM for pyruvate, non-activated form1 Publication
  2. KM=12 mM for pyruvate, activated form1 Publication

    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 sitei50Thiamine pyrophosphateUniRule annotationCombined sources1 Publication1
    Binding sitei210FADCombined sources1 Publication1
    Binding sitei292FADUniRule annotationCombined sources1 Publication1
    Binding sitei297FADCombined sources1 Publication1
    Binding sitei382Thiamine pyrophosphateCombined sources1 Publication1
    <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 bindingi433MagnesiumUniRule annotationCombined sources1 Publication1
    Metal bindingi460MagnesiumUniRule annotationCombined sources1 Publication1
    Metal bindingi462Magnesium; via carbonyl oxygenCombined 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>Sitei465Moves into active site upon enzyme activation, plays a role in electron transferUniRule annotation1 Publication1
    Sitei549 – 550In vitro cleavage to yield alpha-peptide1 Publication2

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi234 – 235FADCombined sources1 Publication2
    Nucleotide bindingi251 – 254FADUniRule annotationCombined sources1 Publication4
    Nucleotide bindingi274 – 278FADUniRule annotationCombined sources1 Publication5
    Nucleotide bindingi311 – 312FADCombined sources1 Publication2
    Nucleotide bindingi403 – 404FADCombined sources1 Publication2

    <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 functionOxidoreductase
    LigandFAD, Flavoprotein, Lipid-binding, Magnesium, Metal-binding, Nucleotide-binding, Pyruvate, Thiamine pyrophosphate, Ubiquinone

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:PYRUVOXID-MONOMER
    ECOL316407:JW0855-MONOMER
    MetaCyc:PYRUVOXID-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.2.5.1 2026

    <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:
    Pyruvate dehydrogenase [ubiquinone]UniRule annotation (EC:1.2.5.1UniRule annotation2 Publications)
    Alternative name(s):
    Pyruvate oxidaseUniRule annotation
    Short name:
    POXUniRule annotation
    Pyruvate:ubiquinone-8 oxidoreductaseUniRule 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:poxBUniRule annotation
    Ordered Locus Names:b0871, JW0855
    <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

    Cell inner membrane, Cell membrane, Membrane

    <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

    Not essential it can be deleted.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>Mutagenesisi533A → T in poxB11; poor activity in vivo, no longer activated by lipids. 1 Publication1
    Mutagenesisi549 – 572Missing in poxB6. Inactive in vivo, does not complement inactive mutants. Active in vitro, no longer activated by nor binds to, detergents. 2 PublicationsAdd BLAST24
    Mutagenesisi553A → V in poxB14; poor activity in vivo, no longer activated by lipids. 1 Publication1
    Mutagenesisi560D → P in poxB15; normal activity. 1 Publication1
    Mutagenesisi564 – 572Missing in poxB7 Inactive in vivo, reduced activity in vitro. 1 Publication9
    Mutagenesisi564E → P in poxB16; loss of activity, weakly activated by cleavage. 1 Publication1
    Mutagenesisi570 – 572Missing in poxB8; reduced activity in vitro, not activated by lipids. 1 Publication3
    Mutagenesisi572R → G in poxB10; reduced activity in vivo and in vitro; may interact less with membranes. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3380

    Drug and drug target database

    More...
    DrugBanki
    DB00336 Nitrofural

    <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_00000446061 – 572Pyruvate dehydrogenase [ubiquinone]Add BLAST572

    <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

    Activated by limited proteolytic digestion in vitro. This cleavage produces a peptide (alpha-peptide) and mimics the activation of enzyme by phospholipids (PubMed:5336022, PubMed:3902830, PubMed:334770, PubMed:334771). Protease activation and lipid-activation are mutually exclusive. Proteolytic cleavage results in the loss of the high affinity lipid-binding site of the enzyme; the cleaved protein is no longer activated by lipids or detergents (PubMed:334771, PubMed:2663858). The proteolytically cleaved enzyme does not represent a functional cleavage in vivo (PubMed:3527254).6 Publications

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P07003

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

    More...
    PaxDbi
    P07003

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P07003

    2D gel databases

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

    More...
    SWISS-2DPAGEi
    P07003

    <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

    Activity is maximal in late exponential and early stationary phase (at protein level) (PubMed:8022274, PubMed:16080684). Expression increases at pH 6.0 (PubMed:16080684). Under control of rpoS (at protein level). Transcribed at lower levels during anaerobic growth (PubMed:8022274).2 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 annotation1 Publication2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    P07003
    With#Exp.IntAct
    itself3EBI-909338,EBI-909338

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4262101, 20 interactors
    850492, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-36216N

    Protein interaction database and analysis system

    More...
    IntActi
    P07003, 4 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0871

    <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

    1572
    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
    P07003

    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
    P07003

    <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>Regioni1 – 182Pyr domainUniRule annotation1 PublicationAdd BLAST182
    Regioni183 – 334FAD-binding domainUniRule annotation1 PublicationAdd BLAST152
    Regioni335 – 530PP-binding domainUniRule annotation1 PublicationAdd BLAST196
    Regioni406 – 408Thiamine pyrophosphate bindingUniRule annotationCombined sources1 Publication3
    Regioni433 – 435Thiamine pyrophosphate bindingUniRule annotationCombined sources1 Publication3
    Regioni460 – 466Thiamine pyrophosphate bindingUniRule annotationCombined sources1 Publication7
    Regioni531 – 572Membrane-binding domainUniRule annotation1 PublicationAdd BLAST42

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region, which includes the in vitro-derived alpha-peptide (residues 550-572). The C-terminus is held closely against the rest of the protein and covers the active site; during activation it detaches from the rest of the protein and folds into an amphipathic helix upon membrane binding. Comparison of full-length and proteolyzed structures shows activation is a result of conformational changes that expose the active site.1 Publication

    <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 TPP enzyme family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C7K Bacteria
    COG0028 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_013748_3_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P07003

    KEGG Orthology (KO)

    More...
    KOi
    K00156

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P07003

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00850 POX, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR029061 THDP-binding
    IPR012000 Thiamin_PyroP_enz_cen_dom
    IPR012001 Thiamin_PyroP_enz_TPP-bd_dom
    IPR000399 TPP-bd_CS
    IPR011766 TPP_enzyme-bd_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02775 TPP_enzyme_C, 1 hit
    PF00205 TPP_enzyme_M, 1 hit
    PF02776 TPP_enzyme_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52467 SSF52467, 1 hit
    SSF52518 SSF52518, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00187 TPP_ENZYMES, 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.

    P07003-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKQTVAAYIA KTLESAGVKR IWGVTGDSLN GLSDSLNRMG TIEWMSTRHE
    60 70 80 90 100
    EVAAFAAGAE AQLSGELAVC AGSCGPGNLH LINGLFDCHR NHVPVLAIAA
    110 120 130 140 150
    HIPSSEIGSG YFQETHPQEL FRECSHYCEL VSSPEQIPQV LAIAMRKAVL
    160 170 180 190 200
    NRGVSVVVLP GDVALKPAPE GATMHWYHAP QPVVTPEEEE LRKLAQLLRY
    210 220 230 240 250
    SSNIALMCGS GCAGAHKELV EFAGKIKAPI VHALRGKEHV EYDNPYDVGM
    260 270 280 290 300
    TGLIGFSSGF HTMMNADTLV LLGTQFPYRA FYPTDAKIIQ IDINPASIGA
    310 320 330 340 350
    HSKVDMALVG DIKSTLRALL PLVEEKADRK FLDKALEDYR DARKGLDDLA
    360 370 380 390 400
    KPSEKAIHPQ YLAQQISHFA ADDAIFTCDV GTPTVWAARY LKMNGKRRLL
    410 420 430 440 450
    GSFNHGSMAN AMPQALGAQA TEPERQVVAM CGDGGFSMLM GDFLSVVQMK
    460 470 480 490 500
    LPVKIVVFNN SVLGFVAMEM KAGGYLTDGT ELHDTNFARI AEACGITGIR
    510 520 530 540 550
    VEKASEVDEA LQRAFSIDGP VLVDVVVAKE ELAIPPQIKL EQAKGFSLYM
    560 570
    LRAIISGRGD EVIELAKTNW LR
    Length:572
    Mass (Da):62,011
    Last modified:April 1, 1988 - 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:i57B38B9E3A92BDEA
    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 conflicti364 – 365QQ → HE in AAB59101 (PubMed:2663858).Curated2
    Sequence conflicti364 – 365QQ → HE in AAB59102 (PubMed:2663858).Curated2
    Sequence conflicti414 – 416QAL → HGV in AAB59101 (PubMed:2663858).Curated3
    Sequence conflicti414 – 416QAL → HGV in AAB59102 (PubMed:2663858).Curated3

    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
    X04105 Genomic DNA Translation: CAA27725.1
    U00096 Genomic DNA Translation: AAC73958.1
    AP009048 Genomic DNA Translation: BAA35585.1
    S73268 Genomic DNA Translation: AAB31180.1
    M28208 Genomic DNA Translation: AAB59101.1
    L47688 Genomic DNA Translation: AAB59102.1
    L47689 Genomic DNA Translation: AAB59103.1
    L47690 Genomic DNA Translation: AAB59104.1
    L47691 Genomic DNA Translation: AAB59105.1
    L47692 Genomic DNA Translation: AAB59106.1
    L47693 Genomic DNA Translation: AAB59107.1
    L47694 Genomic DNA Translation: AAB59108.1
    L47695 Genomic DNA Translation: AAB59109.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A23648 DEECPC

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415392.1, NC_000913.3
    WP_000815337.1, NZ_SSZK01000002.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73958; AAC73958; b0871
    BAA35585; BAA35585; BAA35585

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946132

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0855
    eco:b0871

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1406

    <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
    X04105 Genomic DNA Translation: CAA27725.1
    U00096 Genomic DNA Translation: AAC73958.1
    AP009048 Genomic DNA Translation: BAA35585.1
    S73268 Genomic DNA Translation: AAB31180.1
    M28208 Genomic DNA Translation: AAB59101.1
    L47688 Genomic DNA Translation: AAB59102.1
    L47689 Genomic DNA Translation: AAB59103.1
    L47690 Genomic DNA Translation: AAB59104.1
    L47691 Genomic DNA Translation: AAB59105.1
    L47692 Genomic DNA Translation: AAB59106.1
    L47693 Genomic DNA Translation: AAB59107.1
    L47694 Genomic DNA Translation: AAB59108.1
    L47695 Genomic DNA Translation: AAB59109.1
    PIRiA23648 DEECPC
    RefSeqiNP_415392.1, NC_000913.3
    WP_000815337.1, NZ_SSZK01000002.1

    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
    3EY9X-ray2.90A/B1-572[»]
    3EYAX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-549[»]
    SMRiP07003
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4262101, 20 interactors
    850492, 1 interactor
    DIPiDIP-36216N
    IntActiP07003, 4 interactors
    STRINGi511145.b0871

    Chemistry databases

    ChEMBLiCHEMBL3380
    DrugBankiDB00336 Nitrofural

    2D gel databases

    SWISS-2DPAGEiP07003

    Proteomic databases

    jPOSTiP07003
    PaxDbiP07003
    PRIDEiP07003

    Genome annotation databases

    EnsemblBacteriaiAAC73958; AAC73958; b0871
    BAA35585; BAA35585; BAA35585
    GeneIDi946132
    KEGGiecj:JW0855
    eco:b0871
    PATRICifig|1411691.4.peg.1406

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0747

    Phylogenomic databases

    eggNOGiENOG4105C7K Bacteria
    COG0028 LUCA
    HOGENOMiCLU_013748_3_0_6
    InParanoidiP07003
    KOiK00156
    PhylomeDBiP07003

    Enzyme and pathway databases

    BioCyciEcoCyc:PYRUVOXID-MONOMER
    ECOL316407:JW0855-MONOMER
    MetaCyc:PYRUVOXID-MONOMER
    BRENDAi1.2.5.1 2026

    Miscellaneous databases

    EvolutionaryTraceiP07003

    Protein Ontology

    More...
    PROi
    PR:P07003

    Family and domain databases

    HAMAPiMF_00850 POX, 1 hit
    InterProiView protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR029061 THDP-binding
    IPR012000 Thiamin_PyroP_enz_cen_dom
    IPR012001 Thiamin_PyroP_enz_TPP-bd_dom
    IPR000399 TPP-bd_CS
    IPR011766 TPP_enzyme-bd_C
    PfamiView protein in Pfam
    PF02775 TPP_enzyme_C, 1 hit
    PF00205 TPP_enzyme_M, 1 hit
    PF02776 TPP_enzyme_N, 1 hit
    SUPFAMiSSF52467 SSF52467, 1 hit
    SSF52518 SSF52518, 2 hits
    PROSITEiView protein in PROSITE
    PS00187 TPP_ENZYMES, 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 nameiPOXB_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: P07003
    Secondary accession number(s): Q47513
    , Q47514, Q47515, Q47516, Q47517, Q47518, Q47519, Q47520
    <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: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: June 17, 2020
    This is version 170 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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