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UniProtKB - P07003 (POXB_ECOLI)

Entry version 177 (25 May 2022)
Sequence version 1 (01 Apr 1988)
Previous versions | rss
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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

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 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

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 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

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

<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">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

Complete GO annotation on QuickGO ...

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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P07003

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		COG0028, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_013748_3_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07003

Identification of Orthologs from Complete Genome Data

More...OMAi		YEATHEC

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
IPR044261, PoxB-like
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[»]
AlphaFoldDBiP07003
SMRiP07003
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

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

Chemistry databases

ChEMBLiCHEMBL3380

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

eggNOGiCOG0028, Bacteria
HOGENOMiCLU_013748_3_0_6
InParanoidiP07003
OMAiYEATHEC
PhylomeDBiP07003

Enzyme and pathway databases

BioCyciEcoCyc: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
IPR044261, PoxB-like
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

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: May 25, 2022
This is version 177 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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