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Entry version 102 (02 Jun 2021)
Sequence version 1 (01 Oct 2002)
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Protein

Fructose-1,6-bisphosphate aldolase/phosphatase

Gene

fbp

Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P) (PubMed:12065581, PubMed:20348906).

Does not display hydrolase activity against fructose 2,6-bisphosphate, fructose 6-phosphate, fructose 1-phosphate, glucose 6-phosphate, and glucose 1-phosphate (PubMed:12065581).

Exhibits only negligible activity on inositol-1-phosphate (IMP) (PubMed:15317785).

Is essential for the growth of T.kodakaraensis under gluconeogenic conditions (PubMed:15317785).

3 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

Mg2+1 Publication

<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

Activity is enhanced by dithioerythritol, and is slightly inhibited by fructose 2,6-bisphosphate. AMP does not inhibit the enzyme activity.1 Publication

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

kcat is 17 sec(-1) for the FBPase activity (at 95 degrees Celsius). kcat is 7 sec(-1) for the FBPase activity (at 85 degrees Celsius). kcat is 2.9 sec(-1) for the FBPase activity (at 37 degrees Celsius).1 Publication
  1. KM=100 µM for D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 95 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is over 95 degrees Celsius. The enzyme shows a nearly linear increase in activity between 37 and 95 degrees Celsius, with a 6-fold increase between these temperatures. Is highly thermostable, displaying a half-life of 150 minutes in boiling water.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.1 Publication1 Publication
    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%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei15Proton acceptor; for FBP phosphatase activityBy similarity1
    <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 bindingi15Magnesium 1By similarity1
    Metal bindingi22Magnesium 1; via pros nitrogenBy similarity1
    <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 sitei22DHAP; via tele nitrogenBy similarity1
    Binding sitei22FBP; via tele nitrogenBy similarity1
    Metal bindingi56Magnesium 1By similarity1
    Metal bindingi56Magnesium 2By similarity1
    Metal bindingi57Magnesium 2By similarity1
    Binding sitei94FBPBy similarity1
    Metal bindingi98Magnesium 1By similarity1
    Metal bindingi135Magnesium 2By similarity1
    Binding sitei136DHAPBy similarity1
    Binding sitei136FBPBy similarity1
    Active sitei237Proton donor/acceptor; for FBP aldolase activityBy similarity1
    Active sitei240Schiff-base intermediate with DHAP; for FBP aldolase activityBy similarity1
    Metal bindingi240Magnesium 3; via carbonyl oxygenBy similarity1
    Metal bindingi241Magnesium 3By similarity1
    Metal bindingi241Magnesium 4By similarity1
    Metal bindingi242Magnesium 2By similarity1
    Metal bindingi242Magnesium 3By similarity1
    Binding sitei274DHAP; via amide nitrogenBy similarity1
    Binding sitei274FBP; via amide nitrogenBy similarity1
    Binding sitei295DHAPBy similarity1
    Binding sitei295FBPBy similarity1
    Binding sitei357FBPBy similarity1

    <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 functionHydrolase, Lyase
    Biological processCarbohydrate metabolism, Gluconeogenesis
    LigandMagnesium, Metal-binding, Schiff base

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    TKOD69014:G1G2A-2184-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.3.11, 5246

    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%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:
    Fructose-1,6-bisphosphate aldolase/phosphatase1 Publication (EC:3.1.3.112 Publications, EC:4.1.2.131 Publication)
    Short name:
    FBP A/PUniRule annotation
    Short name:
    FBP aldolase/phosphatase1 Publication
    Alternative name(s):
    Fructose-1,6-bisphosphatase1 Publication
    Short name:
    FBPase1 Publication
    <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:fbp1 Publication
    Ordered Locus Names:TK2164Imported
    <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>OrganismiThermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
    <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 identifieri69014 [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 lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    <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
    • UP000000536 <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

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene cannot grow under gluconeogenic conditions while glycolytic growth is unimpaired, and the gene disruption results in the complete abolishment of intracellular FBPase activity.1 Publication

    <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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00004371852 – 375Fructose-1,6-bisphosphate aldolase/phosphataseAdd BLAST374

    <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

    High levels of transcripts are detected in cells grown on pyruvate or amino acids, whereas no transcription is detected when starch is present in the medium, revealing a sugar-repressed gene expression.1 Publication

    <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

    Homooctamer; dimer of tetramers.

    By similarity1 Publication

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    Q8NKR9, 1 interactor

    Molecular INTeraction database

    More...
    MINTi
    Q8NKR9

    STRING: functional protein association networks

    More...
    STRINGi
    69014.TK2164

    <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

    3D structure databases

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

    More...
    SMRi
    Q8NKR9

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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>Regioni107 – 108FBP bindingBy similarity2
    Regioni250 – 251FBP binding; shared with dimeric partnerBy similarity2

    <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

    Consists of a single catalytic domain, but remodels its active-site architecture via a large structural change to exhibit dual activities.By similarity

    <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 FBP aldolase/phosphatase family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG04180, Archaea

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_041630_0_0_2

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q8NKR9

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YMRRHGP

    Database of Orthologous Groups

    More...
    OrthoDBi
    21175at2157

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02067, FBP_aldolase_phosphatase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002803, FBPase_V
    IPR036076, FBPase_V_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR38341, PTHR38341, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01950, FBPase_3, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF015647, FBPtase_archl, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF111249, SSF111249, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00159, ALDOLASE_KDPG_KHG_1, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8NKR9-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAVGDKITIS VIKADIGGWP GHSRVHPQLV ETAEDVLSKA VEDGTIIDFY
    60 70 80 90 100
    VATCGDDLQL IMTHKRGVDS PDIHGLAWKA FEEATKVAKE LGLYGAGQDL
    110 120 130 140 150
    LKDAFSGNVR GMGPGVAEME ITLRKSEPVV TFHMDKTEPG AFNLPIFRMF
    160 170 180 190 200
    ADPFNTAGLI IDPKMHMGFR FEVWDILEHK RVILNTPEEL YDLLALIGAK
    210 220 230 240 250
    SRYVIKRVYP KPGHPIPENE PVAVVSTEKL YEVAGEYVGK DDPVAIVRAQ
    260 270 280 290 300
    SGLPALGEVL EPFAFPHLVS GWMRGSHNGP LMPVPMHQAN PTRFDGPPRV
    310 320 330 340 350
    VALGWQISPE GKLVGPVDLF DDPAFDYARQ KALEITEYMR RHGPFEPHRL
    360 370
    PLEEMEYTTL PGVLKRLTDR FEPIE
    Length:375
    Mass (Da):41,661
    Last modified:October 1, 2002 - 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:i1552ED57CF19EE93
    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
    AB081839 Genomic DNA Translation: BAC10571.1
    AP006878 Genomic DNA Translation: BAD86353.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011251114.1, NC_006624.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAD86353; BAD86353; TK2164

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3235025

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    tko:TK2164

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|69014.16.peg.2119

    <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
    AB081839 Genomic DNA Translation: BAC10571.1
    AP006878 Genomic DNA Translation: BAD86353.1
    RefSeqiWP_011251114.1, NC_006624.1

    3D structure databases

    SMRiQ8NKR9
    ModBaseiSearch...

    Protein-protein interaction databases

    IntActiQ8NKR9, 1 interactor
    MINTiQ8NKR9
    STRINGi69014.TK2164

    Genome annotation databases

    EnsemblBacteriaiBAD86353; BAD86353; TK2164
    GeneIDi3235025
    KEGGitko:TK2164
    PATRICifig|69014.16.peg.2119

    Phylogenomic databases

    eggNOGiarCOG04180, Archaea
    HOGENOMiCLU_041630_0_0_2
    InParanoidiQ8NKR9
    OMAiYMRRHGP
    OrthoDBi21175at2157

    Enzyme and pathway databases

    UniPathwayiUPA00138
    BioCyciTKOD69014:G1G2A-2184-MONOMER
    BRENDAi3.1.3.11, 5246

    Family and domain databases

    HAMAPiMF_02067, FBP_aldolase_phosphatase, 1 hit
    InterProiView protein in InterPro
    IPR002803, FBPase_V
    IPR036076, FBPase_V_sf
    PANTHERiPTHR38341, PTHR38341, 1 hit
    PfamiView protein in Pfam
    PF01950, FBPase_3, 1 hit
    PIRSFiPIRSF015647, FBPtase_archl, 1 hit
    SUPFAMiSSF111249, SSF111249, 1 hit
    PROSITEiView protein in PROSITE
    PS00159, ALDOLASE_KDPG_KHG_1, 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 nameiFBPAP_THEKO
    <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: Q8NKR9
    Secondary accession number(s): Q5JHJ3
    <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: September 7, 2016
    Last sequence update: October 1, 2002
    Last modified: June 2, 2021
    This is version 102 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

    Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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