Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamine synthetase

Gene

glnA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.1 Publication

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

Enzyme 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

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
    Metal bindingi132Manganese 1Combined sources1 Publication1
    Metal bindingi134Magnesium 2Combined sources1 Publication1
    Binding sitei210ATPCombined sources1 Publication1
    Metal bindingi215Magnesium 2Combined sources1 Publication1
    Metal bindingi223Magnesium 2Combined sources1 Publication1
    Binding sitei268L-glutamate; via oxygen carbonylBy 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
    Nucleotide bindingi274 – 276ATPBy similarity3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

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

    Enzyme and pathway databases

    BRENDAi6.3.1.2. 382.

    Names & Taxonomyi

    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
    Gene namesi
    Name:glnA1 Publication
    Ordered Locus Names:slr1756
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
    Proteomesi
    • UP000001425 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm By similarity

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001532721 – 473Glutamine synthetaseAdd BLAST473

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei401O-AMP-tyrosineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP77961.

    Expressioni

    Inductioni

    Highly expressed in nitrate- or ammonium-grown cells and exhibits two- to fourfold-higher expression in nitrogen-starved cells.1 Publication

    Interactioni

    Subunit structurei

    Oligomer of 12 subunits arranged in the form of two hexagons.1 Publication

    Protein-protein interaction databases

    DIPiDIP-48822N.
    IntActiP77961. 4 interactors.

    Structurei

    Secondary structure

    1473
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi5 – 14Combined sources10
    Beta strandi19 – 25Combined sources7
    Beta strandi27 – 29Combined sources3
    Beta strandi31 – 37Combined sources7
    Helixi38 – 40Combined sources3
    Helixi43 – 46Combined sources4
    Beta strandi50 – 53Combined sources4
    Helixi63 – 65Combined sources3
    Beta strandi67 – 72Combined sources6
    Helixi74 – 76Combined sources3
    Beta strandi87 – 95Combined sources9
    Turni97 – 99Combined sources3
    Beta strandi100 – 102Combined sources3
    Helixi107 – 120Combined sources14
    Beta strandi121 – 123Combined sources3
    Beta strandi125 – 133Combined sources9
    Beta strandi135 – 145Combined sources11
    Beta strandi150 – 155Combined sources6
    Helixi160 – 162Combined sources3
    Turni186 – 188Combined sources3
    Helixi192 – 204Combined sources13
    Beta strandi209 – 214Combined sources6
    Turni218 – 220Combined sources3
    Beta strandi221 – 226Combined sources6
    Helixi231 – 251Combined sources21
    Beta strandi255 – 257Combined sources3
    Beta strandi271 – 279Combined sources9
    Beta strandi286 – 289Combined sources4
    Helixi290 – 292Combined sources3
    Helixi295 – 315Combined sources21
    Helixi321 – 324Combined sources4
    Turni327 – 329Combined sources3
    Beta strandi337 – 340Combined sources4
    Beta strandi344 – 348Combined sources5
    Helixi355 – 357Combined sources3
    Beta strandi360 – 362Combined sources3
    Helixi371 – 388Combined sources18
    Helixi418 – 427Combined sources10
    Helixi430 – 433Combined sources4
    Beta strandi436 – 438Combined sources3
    Helixi440 – 453Combined sources14
    Helixi455 – 460Combined sources6
    Helixi465 – 470Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NG0X-ray2.80A1-473[»]
    ProteinModelPortaliP77961.
    SMRiP77961.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni267 – 268L-glutamate bindingBy similarity2

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000005157.
    InParanoidiP77961.
    KOiK01915.
    PhylomeDBiP77961.

    Family and domain databases

    Gene3Di3.10.20.70. 1 hit.
    3.30.590.10. 1 hit.
    InterProiView protein in InterPro
    IPR008147. Gln_synt_b-grasp.
    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.
    TIGRFAMsiTIGR00653. GlnA. 1 hit.
    PROSITEiView protein in PROSITE
    PS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.

    Sequencei

    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
    Checksum:i75F8E28EB5EA9515
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X69199 Genomic DNA. Translation: CAA49139.1.
    BA000022 Genomic DNA. Translation: BAA17055.1.
    PIRiS75141.

    Genome annotation databases

    EnsemblBacteriaiBAA17055; BAA17055; BAA17055.
    KEGGisyn:slr1756.

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NG0X-ray2.80A1-473[»]
    ProteinModelPortaliP77961.
    SMRiP77961.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48822N.
    IntActiP77961. 4 interactors.

    Proteomic databases

    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.
    3.30.590.10. 1 hit.
    InterProiView protein in InterPro
    IPR008147. Gln_synt_b-grasp.
    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.
    TIGRFAMsiTIGR00653. GlnA. 1 hit.
    PROSITEiView protein in PROSITE
    PS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGLN1B_SYNY3
    AccessioniPrimary (citable) accession number: P77961
    Secondary accession number(s): Q59981
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: June 7, 2017
    This is version 108 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.