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Entry version 118 (08 May 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Glutamine synthetase

Gene

glnA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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

Involved in nitrogen metabolism via ammonium assimilation (PubMed:8002575). Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:1973929, PubMed:8002575).2 Publications

<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+2 PublicationsNote: Binds 2 Mg2+ ions per subunit (Ref.6). Also able to bind Co2+, Mn2+ and Ca2+ ion (PubMed:1973929).2 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

Inhibited by ADP (90%), AMP (80%), alanine (52%) and aspartate (41%) (PubMed:1973929). The activity of this enzyme could be controlled by adenylation under conditions of abundant glutamine (By similarity).By similarity1 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=0.17 mM for ammonium1 Publication
  2. KM=0.55 mM for ATP1 Publication
  3. KM=1.2 mM for L-glutamate1 Publication
  4. KM=14.3 mM for L-glutamine1 Publication
  5. KM=14.5 mM for hydroxylamine1 Publication

    pH dependencei

    Optimum pH is 7.2.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi132Manganese 1Combined sources1 Publication1
    Metal bindingi134Magnesium 2Combined sources1 Publication1
    <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 sitei210ATPCombined sources1 Publication1
    Metal bindingi215Magnesium 2Combined sources1 Publication1
    Metal bindingi223Magnesium 2Combined sources1 Publication1
    Binding sitei268L-glutamate; via carbonyl oxygenBy similarity1
    Metal bindingi272Magnesium 1; via pros nitrogenBy similarity1
    Binding sitei276ATPCombined sources1 Publication1
    Binding sitei324L-glutamateBy similarity1
    Binding sitei330L-glutamateBy similarity1
    Binding sitei342ATPCombined sources1 Publication1
    Binding sitei342L-glutamateBy similarity1
    Binding sitei347ATPCombined sources1 Publication1
    Binding sitei356ATPCombined sources1 Publication1
    Metal bindingi361Manganese 1Combined sources1 Publication1
    Binding sitei363L-glutamateBy similarity1

    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 bindingi274 – 276ATPBy similarity3

    <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 functionLigase
    LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.3.1.2 382

    <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:
    Glutamine synthetase1 Publication (EC:6.3.1.21 Publication)
    Short name:
    GS1 Publication
    Alternative name(s):
    Glutamate--ammonia ligaseCurated
    Glutamine synthetase I betaCurated
    Short name:
    GSI betaCurated
    <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:glnA1 Publication
    Ordered Locus Names:slr1756
    <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>OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    <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 identifieri1111708 [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 lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
    <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
    • UP000001425 <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

    <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 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 are able to grow with nitrate as the sole nitrogen source, but it are unable to grow in ammonium-containing medium. This mutant is impaired in the regulation of the nitrate assimilation system.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 ‘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_00001532721 – 473Glutamine synthetaseAdd BLAST473

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei401O-AMP-tyrosineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

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

    More...
    PaxDbi
    P77961

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P77961

    <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

    Highly expressed in nitrate- or ammonium-grown cells and exhibits two- to fourfold-higher expression in nitrogen-starved cells.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_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

    Oligomer of 12 subunits arranged in the form of two hexagons.

    1 Publication

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-48822N

    Protein interaction database and analysis system

    More...
    IntActi
    P77961, 5 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    1148.1652131

    <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

    1473
    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
    P77961

    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>Regioni267 – 268L-glutamate bindingBy similarity2

    <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 glutamine synthetase family.Curated

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000005157

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P77961

    KEGG Orthology (KO)

    More...
    KOi
    K01915

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P77961

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.20.70, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008147 Gln_synt_b-grasp
    IPR036651 Gln_synt_N
    IPR014746 Gln_synth/guanido_kin_cat_dom
    IPR008146 Gln_synth_cat_dom
    IPR027303 Gln_synth_gly_rich_site
    IPR004809 Gln_synth_I
    IPR027302 Gln_synth_N_conserv_site

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00120 Gln-synt_C, 1 hit
    PF03951 Gln-synt_N, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01230 Gln-synt_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF54368 SSF54368, 1 hit
    SSF55931 SSF55931, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00653 GlnA, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00180 GLNA_1, 1 hit
    PS00181 GLNA_ATP, 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.

    P77961-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MARTPQEVLK WIQDENIKII DLKFIDTPGI WQHCSFYYDQ LDENSFTEGI
    60 70 80 90 100
    PFDGSSIRGW KAINESDMCM VPDPNTATID PFCKEPTLSM ICSIKEPRTG
    110 120 130 140 150
    EWYNRDPRTI AAKAVEYLRG TGIADTVYFG PEAEFFLFDD IRFGQTENSS
    160 170 180 190 200
    YYFADSVEGR WNTGREEEGG NLGYKPGYKQ GYFPVAPTDT AQDIRTEMLL
    210 220 230 240 250
    TMAGLCVPIE KHHHEVASGG QNELGIKFDK LVNSADNLMI YKYVIKNVAK
    260 270 280 290 300
    KYGKTVTFMP KPIFNDNGSG MHVHQSLWKD GQPLFAGDKY AGFSQMGLWY
    310 320 330 340 350
    IGGILKHAPA LLAFTNPTTN SYKRLVPGFE APVNLAYSQG NRSASVRIPL
    360 370 380 390 400
    SGGNPKAKRL EFRCPDATSN PYLAFAAMLC AGIDGIKNQI DPGEPLDVDI
    410 420 430 440 450
    YDLSPEELAK IPSTPGSLEA ALEALEKDHE FLTGTGVFSP DFVESWIEYK
    460 470
    LDNEVNPMRL RPHPYEFSLY YDC
    Length:473
    Mass (Da):53,026
    Last modified:November 1, 1997 - 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:i75F8E28EB5EA9515
    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 conflicti115V → A in BAA17055 (PubMed:8905231).Curated1
    Sequence conflicti145 – 147QTE → PNG in CAA49139 (PubMed:7727755).Curated3
    Sequence conflicti180Q → E in CAA49139 (PubMed:7727755).Curated1
    Sequence conflicti204 – 206GLC → AFG in BAA17055 (PubMed:8905231).Curated3
    Sequence conflicti230K → KFDK in CAA49139 (PubMed:7727755).Curated1
    Sequence conflicti239M → I in CAA49139 (PubMed:7727755).Curated1
    Sequence conflicti358K → N in CAA49139 (PubMed:7727755).Curated1
    Sequence conflicti378 – 379ML → IV in CAA49139 (PubMed:7727755).Curated2
    Sequence conflicti430E → Q in CAA49139 (PubMed:7727755).Curated1

    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
    X69199 Genomic DNA Translation: CAA49139.1
    BA000022 Genomic DNA Translation: BAA17055.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S75141

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAA17055; BAA17055; BAA17055

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    syn:slr1756

    <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
    X69199 Genomic DNA Translation: CAA49139.1
    BA000022 Genomic DNA Translation: BAA17055.1
    PIRiS75141

    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
    3NG0X-ray2.80A1-473[»]
    SMRiP77961
    ModBaseiSearch...

    Protein-protein interaction databases

    DIPiDIP-48822N
    IntActiP77961, 5 interactors
    STRINGi1148.1652131

    Proteomic databases

    PaxDbiP77961
    PRIDEiP77961

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAA17055; BAA17055; BAA17055
    KEGGisyn:slr1756

    Phylogenomic databases

    HOGENOMiHOG000005157
    InParanoidiP77961
    KOiK01915
    PhylomeDBiP77961

    Enzyme and pathway databases

    BRENDAi6.3.1.2 382

    Family and domain databases

    Gene3Di3.10.20.70, 1 hit
    InterProiView protein in InterPro
    IPR008147 Gln_synt_b-grasp
    IPR036651 Gln_synt_N
    IPR014746 Gln_synth/guanido_kin_cat_dom
    IPR008146 Gln_synth_cat_dom
    IPR027303 Gln_synth_gly_rich_site
    IPR004809 Gln_synth_I
    IPR027302 Gln_synth_N_conserv_site
    PfamiView protein in Pfam
    PF00120 Gln-synt_C, 1 hit
    PF03951 Gln-synt_N, 1 hit
    SMARTiView protein in SMART
    SM01230 Gln-synt_C, 1 hit
    SUPFAMiSSF54368 SSF54368, 1 hit
    SSF55931 SSF55931, 1 hit
    TIGRFAMsiTIGR00653 GlnA, 1 hit
    PROSITEiView protein in PROSITE
    PS00180 GLNA_1, 1 hit
    PS00181 GLNA_ATP, 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 nameiGLN1B_SYNY3
    <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: P77961
    Secondary accession number(s): Q59981
    <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: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: May 8, 2019
    This is version 118 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

    3D-structure, Complete proteome, 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. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names
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