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Entry version 116 (02 Dec 2020)
Sequence version 2 (18 Apr 2006)
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Protein

Fructose-1,6-bisphosphatase class 1

Gene

fbp

Organism
Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Status
Reviewed-Annotation score:

Annotation score:4 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 only the formation of fructose 6-phosphate by hydrolysis of fructose 1,6-bisphosphate.

1 Publication

<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+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

<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

Not inhibited by AMP and slightly innibited by hydrogen peroxyde.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

  1. KM=25 µM for fructose 1,6-bisphosphate (at pH 8)1 Publication

    pH dependencei

    Optimum pH is 9. Activities at pH 8.0 and 9.5 were approx 67% and 85%, respectively, of that at pH 9.0.1 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: Calvin cycle

    This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway Calvin cycle 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 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 bindingi107Magnesium 1By similarity1
    Metal bindingi129Magnesium 1By similarity1
    Metal bindingi129Magnesium 2By similarity1
    Metal bindingi131Magnesium 1; via carbonyl oxygenBy similarity1
    Metal bindingi132Magnesium 2By 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 sitei224SubstrateBy similarity1
    Binding sitei252SubstrateBy similarity1
    Binding sitei282SubstrateBy similarity1
    Metal bindingi288Magnesium 2By 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
    Biological processCalvin cycle, Carbohydrate metabolism
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    SYNEL:SYNPCC7942_2335-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.3.11, 325

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

    More...
    UniPathwayi
    UPA00116

    <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-bisphosphatase class 1 (EC:3.1.3.11)
    Short name:
    FBPase class 1
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
    Fructose-1,6-bisphosphatase F-II
    <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:fbp
    Ordered Locus Names:Synpcc7942_2335
    <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>OrganismiSynechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2)
    <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 identifieri1140 [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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
    <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
    • UP000002717 <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 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

    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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002004891 – 344Fructose-1,6-bisphosphatase class 1Add BLAST344

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q59943

    <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.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    1140.Synpcc7942_2335

    <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
    Q59943

    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

    <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.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0158, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_039977_2_2_3

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QSGLVCR

    Database of Orthologous Groups

    More...
    OrthoDBi
    945770at2

    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
    IPR044015, FBPase_C_dom
    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
    PF18913, FBPase_C, 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%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.

    Q59943-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAQSTTSETH TRDLDRDCTT LSRHVLEQLQ SFSPEAQDLA ALMQRIGLAA
    60 70 80 90 100
    KLIARRLSHA GLVDDALGFT GEINVQGEAV KRMDVYANQV FISVFRQSGL
    110 120 130 140 150
    VCRLASEEME KPYYIPENCP IGRYTLLYDP LDGSANVDVD LNVGSIFAVR
    160 170 180 190 200
    RQEFYDESHE AKDLLQPGDR QIAAGYVLYG ASTLLVYSMG QGVHVFVLDP
    210 220 230 240 250
    SLGEFVLAQS DIQLPNSGQI YSVNEGNFWQ WPEGYRQYIR EMHRREGYSG
    260 270 280 290 300
    RYSGALVADF HRILMQGGVF LYPETVKNPT GKLRLLYEAA PMAFLAEQAG
    310 320 330 340
    GKASDGQKPI LLRQPQALHE RCPLIIGSAA DVDFVEACLA ESVP
    Length:344
    Mass (Da):38,172
    Last modified:April 18, 2006 - v2
    <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:iE4E6EEC414A6BA79
    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 conflicti29L → F in BAA08536 (PubMed:8837735).Curated1
    Sequence conflicti80V → S in BAA08536 (PubMed:8837735).Curated1
    Sequence conflicti229 – 250WQWPE…EGYSG → CSGPKVSPVHPGNASPRRLQ R in BAA08536 (PubMed:8837735).CuratedAdd BLAST22
    Sequence conflicti247G → A in AAA98846 (PubMed:8566707).Curated1
    Sequence conflicti290A → P in BAA08536 (PubMed:8837735).Curated1
    Sequence conflicti320E → R in BAA08536 (PubMed:8837735).Curated1
    Sequence conflicti336 – 344EACLAESVP → DSLLG in BAA08536 (PubMed:8837735).Curated9

    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
    U33285 Genomic DNA Translation: AAA98846.1
    D49680 Genomic DNA Translation: BAA08536.1
    CP000100 Genomic DNA Translation: ABB58365.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011378409.1, NC_007604.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABB58365; ABB58365; Synpcc7942_2335

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    syf:Synpcc7942_2335

    <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
    U33285 Genomic DNA Translation: AAA98846.1
    D49680 Genomic DNA Translation: BAA08536.1
    CP000100 Genomic DNA Translation: ABB58365.1
    RefSeqiWP_011378409.1, NC_007604.1

    3D structure databases

    SMRiQ59943
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi1140.Synpcc7942_2335

    Proteomic databases

    PRIDEiQ59943

    Genome annotation databases

    EnsemblBacteriaiABB58365; ABB58365; Synpcc7942_2335
    KEGGisyf:Synpcc7942_2335

    Phylogenomic databases

    eggNOGiCOG0158, Bacteria
    HOGENOMiCLU_039977_2_2_3
    OMAiQSGLVCR
    OrthoDBi945770at2

    Enzyme and pathway databases

    UniPathwayiUPA00116
    BioCyciSYNEL:SYNPCC7942_2335-MONOMER
    BRENDAi3.1.3.11, 325

    Family and domain databases

    CDDicd00354, FBPase, 1 hit
    HAMAPiMF_01855, FBPase_class1, 1 hit
    InterProiView protein in InterPro
    IPR044015, FBPase_C_dom
    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
    PF18913, FBPase_C, 1 hit
    PIRSFiPIRSF500210, FBPtase, 1 hit
    PIRSF000904, FBPtase_SBPase, 1 hit
    PRINTSiPR00115, F16BPHPHTASE
    PROSITEiView protein in PROSITE
    PS00124, FBPASE, 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 nameiF16PA_SYNE7
    <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: Q59943
    Secondary accession number(s): P96146, Q31KQ4
    <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: November 1, 1997
    Last sequence update: April 18, 2006
    Last modified: December 2, 2020
    This is version 116 of the entry and version 2 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

    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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