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Entry version 126 (16 Oct 2019)
Sequence version 1 (19 Jul 2005)
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Protein

Fructose-1,6-bisphosphatase class 1

Gene

fbp

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Mg2+UniRule annotation2 PublicationsNote: Binds 2 magnesium ions per subunit.UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. Activated by three-carbon carboxylic acids, phosphorylated three-carbon carboxylic acids and sulfate. Strongly activated by phosphoenolpyruvate and citrate. Inhibited by AMP, which affects the turnover of bound substrate and not the affinity for substrate. Allosterically inhibited by glucose 6-phosphate. AMP and glucose 6-phosphate act synergistically as allosteric inhibitors. Phosphoenolpyruvate antagonizes inhibition by AMP and glucose 6-phosphate. Fructose 2,6-bisphosphate acts as competitive inhibitor.4 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

  1. KM=1.7 µM for fructose 1,6-biphosphate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei30Allosteric activator2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi89Magnesium 1UniRule annotation1 Publication1
    Metal bindingi110Magnesium 1UniRule annotation1 Publication1
    Metal bindingi110Magnesium 2UniRule annotation2 Publications1
    Metal bindingi112Magnesium 1; via carbonyl oxygenUniRule annotation1 Publication1
    Metal bindingi113Magnesium 2UniRule annotation2 Publications1
    Binding sitei187Allosteric activator; via amide nitrogen2 Publications1
    Binding sitei206SubstrateUniRule annotation2 Publications1
    Binding sitei222Allosteric inhibitor glucose-6-phosphate1 Publication1
    Binding sitei225Allosteric inhibitor glucose-6-phosphate1 Publication1
    Binding sitei239SubstrateUniRule annotation2 Publications1
    Binding sitei269SubstrateUniRule annotation2 Publications1
    Metal bindingi275Magnesium 2UniRule annotation2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi19 – 23AMP1 Publication5
    Nucleotide bindingi104 – 105AMP1 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 functionAllosteric enzyme, Hydrolase
    Biological processCarbohydrate metabolism
    LigandMagnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:F16B-MONOMER
    ECOL316407:JW4191-MONOMER
    MetaCyc:F16B-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.3.11 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0A993

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

    More...
    UniPathwayi
    UPA00138

    <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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase class 1UniRule annotationCurated (EC:3.1.3.11UniRule annotation2 Publications)
    Short name:
    FBPase class 1UniRule annotationCurated
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1UniRule annotationCurated
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:fbp1 Publication
    Synonyms:fdp
    Ordered Locus Names:b4232, JW4191
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10283 fbp

    <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 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002004921 – 332Fructose-1,6-bisphosphatase class 1Add BLAST332

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0A993

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A993

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

    More...
    PaxDbi
    P0A993

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A993

    2D gel databases

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

    More...
    SWISS-2DPAGEi
    P0A993

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer. Phosphoenolpyruvate stabilizes the homotetramer.

    4 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259316, 21 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b4232

    <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

    1332
    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
    P0A993

    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
    P0A993

    <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>Regioni3 – 5Allosteric activator binding2 Publications3
    Regioni113 – 116Substrate bindingUniRule annotation2 Publications4
    Regioni257 – 259Substrate bindingUniRule annotation2 Publications3

    <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 FBPase class 1 family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CZI Bacteria
    COG0158 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000191265

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A993

    KEGG Orthology (KO)

    More...
    KOi
    K03841

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A993

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00354 FBPase, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01855 FBPase_class1, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000146 FBPase_class-1
    IPR033391 FBPase_N
    IPR028343 FBPtase
    IPR020548 Fructose_bisphosphatase_AS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11556 PTHR11556, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00316 FBPase, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF500210 FBPtase, 1 hit
    PIRSF000904 FBPtase_SBPase, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00115 F16BPHPHTASE

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00124 FBPASE, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P0A993-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTLGEFIVE KQHEFSHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG
    60 70 80 90 100
    ASGAENVQGE VQQKLDLFAN EKLKAALKAR DIVAGIASEE EDEIVVFEGC
    110 120 130 140 150
    EHAKYVVLMD PLDGSSNIDV NVSVGTIFSI YRRVTPVGTP VTEEDFLQPG
    160 170 180 190 200
    NKQVAAGYVV YGSSTMLVYT TGCGVHAFTY DPSLGVFCLC QERMRFPEKG
    210 220 230 240 250
    KTYSINEGNY IKFPNGVKKY IKFCQEEDKS TNRPYTSRYI GSLVADFHRN
    260 270 280 290 300
    LLKGGIYLYP STASHPDGKL RLLYECNPMA FLAEQAGGKA SDGKERILDI
    310 320 330
    IPETLHQRRS FFVGNDHMVE DVERFIREFP DA
    Length:332
    Mass (Da):36,834
    Last modified:July 19, 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:i4F0FC8109491D78F
    GO

    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
    X12545 mRNA Translation: CAA31062.1
    U14003 Genomic DNA Translation: AAA97129.1
    U00096 Genomic DNA Translation: AAC77189.1
    AP009048 Genomic DNA Translation: BAE78232.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S01383 PAEC

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418653.1, NC_000913.3
    WP_000853753.1, NZ_STEB01000013.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC77189; AAC77189; b4232
    BAE78232; BAE78232; BAE78232

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948753

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW4191
    eco:b4232

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2470

    <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
    X12545 mRNA Translation: CAA31062.1
    U14003 Genomic DNA Translation: AAA97129.1
    U00096 Genomic DNA Translation: AAC77189.1
    AP009048 Genomic DNA Translation: BAE78232.1
    PIRiS01383 PAEC
    RefSeqiNP_418653.1, NC_000913.3
    WP_000853753.1, NZ_STEB01000013.1

    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
    2GQ1X-ray1.45A1-332[»]
    2OWZX-ray2.18A1-332[»]
    2OX3X-ray2.18A1-332[»]
    2Q8MX-ray2.05A/B1-332[»]
    2QVRX-ray2.18A1-332[»]
    SMRiP0A993
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4259316, 21 interactors
    STRINGi511145.b4232

    2D gel databases

    SWISS-2DPAGEiP0A993

    Proteomic databases

    EPDiP0A993
    jPOSTiP0A993
    PaxDbiP0A993
    PRIDEiP0A993

    Genome annotation databases

    EnsemblBacteriaiAAC77189; AAC77189; b4232
    BAE78232; BAE78232; BAE78232
    GeneIDi948753
    KEGGiecj:JW4191
    eco:b4232
    PATRICifig|1411691.4.peg.2470

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0279
    EcoGeneiEG10283 fbp

    Phylogenomic databases

    eggNOGiENOG4105CZI Bacteria
    COG0158 LUCA
    HOGENOMiHOG000191265
    InParanoidiP0A993
    KOiK03841
    PhylomeDBiP0A993

    Enzyme and pathway databases

    UniPathwayiUPA00138
    BioCyciEcoCyc:F16B-MONOMER
    ECOL316407:JW4191-MONOMER
    MetaCyc:F16B-MONOMER
    BRENDAi3.1.3.11 2026
    SABIO-RKiP0A993

    Miscellaneous databases

    EvolutionaryTraceiP0A993

    Protein Ontology

    More...
    PROi
    PR:P0A993

    Family and domain databases

    CDDicd00354 FBPase, 1 hit
    HAMAPiMF_01855 FBPase_class1, 1 hit
    InterProiView protein in InterPro
    IPR000146 FBPase_class-1
    IPR033391 FBPase_N
    IPR028343 FBPtase
    IPR020548 Fructose_bisphosphatase_AS
    PANTHERiPTHR11556 PTHR11556, 1 hit
    PfamiView protein in Pfam
    PF00316 FBPase, 1 hit
    PIRSFiPIRSF500210 FBPtase, 1 hit
    PIRSF000904 FBPtase_SBPase, 1 hit
    PRINTSiPR00115 F16BPHPHTASE
    PROSITEiView protein in PROSITE
    PS00124 FBPASE, 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 nameiF16PA_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: P0A993
    Secondary accession number(s): P09200, Q2M674
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 16, 2019
    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, Complete proteome, 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
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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