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O08467

- GLNA_THEKO

UniProt

O08467 - GLNA_THEKO

Protein

Glutamine synthetase

Gene

glnA

Organism
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    Carries out the ATP-dependent synthesis of glutamine from ammonium nitrogen and glutamate. Exhibits both L-gamma-glutamylhydroxamate synthetase and gamma-glutamyltransferase activities when using hydroxylamine as substrate; in fact, the enzyme possesses low biosynthetic activity, suggesting that the reaction is biased towards the degradation of glutamine under ammonia-rich conditions. Might play some role in ammonia assimilation under ammonia-starvation conditions. Can also use GTP instead of ATP in the synthetase reaction, but not CTP or UTP.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.By similarity

    Kineticsi

    kcat is 2190 min(-1) towards L-glutamate in the synthetase reaction and 3900 min(-1) towards L-glutamine in the transferase reaction.

    1. KM=23.5 mM for L-glutamate (at pH 7.8 and 60 degrees Celsius)1 Publication
    2. KM=15.2 mM for hydroxylamine (when a high concentration is used, at pH 7.8 and 60 degrees Celsius)1 Publication
    3. KM=1.6 mM for hydroxylamine (when a low concentration is used, at pH 7.8 and 60 degrees Celsius)1 Publication
    4. KM=28.0 mM for ATP (at pH 7.8 and 60 degrees Celsius)1 Publication
    5. KM=5.0 mM for L-glutamine (at pH 7.2 and 60 degrees Celsius)1 Publication
    6. KM=6.3 mM for ADP (at pH 7.2 and 60 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.8 for the synthetase reaction and pH 7.2 for the transferase reaction.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius for both transferase and synthetase activities.1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate-ammonia ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glutamine biosynthetic process Source: InterPro
    2. nitrogen fixation Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciTKOD69014:GH72-1833-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Short name:
    GS
    Alternative name(s):
    Glutamate--ammonia ligase
    Gene namesi
    Name:glnA
    Ordered Locus Names:TK1796
    OrganismiThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
    Taxonomic identifieri69014 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000000536: Chromosome

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Glutamine synthetasePRO_0000153211Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei362 – 3621O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Homododecamer.1 Publication

    Protein-protein interaction databases

    IntActiO08467. 1 interaction.
    MINTiMINT-8377176.
    STRINGi69014.TK1796.

    Structurei

    3D structure databases

    ProteinModelPortaliO08467.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0174.
    HOGENOMiHOG000005156.
    KOiK01915.

    Family and domain databases

    Gene3Di3.10.20.70. 1 hit.
    3.30.590.10. 1 hit.
    InterProiIPR008147. Gln_synt_beta.
    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.
    [Graphical view]
    PfamiPF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF54368. SSF54368. 1 hit.
    TIGRFAMsiTIGR00653. GlnA. 1 hit.
    PROSITEiPS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O08467-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNEIKGIERA VQVEVPRPRF LLLAFTDING SLKGMEIPME RYEEAVEDGV    50
    SFDGSSIPGF EGIEDSDLIF KADPSTYAEI PWEGIGRVYG YIYKGDEPYQ 100
    ADPRGILKRV LERLEKEGLK AHIGPEPEFY IFKKNGTWEL HIPDSGGYFD 150
    LVGLDKAREI RREIALYMPY LGLKPEVLHH EVGKAQHEID FRYDEALRTA 200
    DNIVSFKHVV KAVAELHGYY ATFMPKPIYG FPGNGMHLHI SLWKDGENVF 250
    IGEDGLSDTA LHFIGGILKH AKALAALTNP TVNSYKRLVP GYEAPVYISW 300
    GYRNRSALIR VPAFKGSGAR IEYRCPDPSA NPYLALAGIL MVGLDGIKKK 350
    VEPDSYVETN VYEMDDAERE RLGIDTLPGS LGEALEELKK DKTVREALGG 400
    AYKNFIDYKE REWEEYIEYL SSRDIPIDTK KVTEWELERY FYV 443
    Length:443
    Mass (Da):50,308
    Last modified:March 29, 2005 - v2
    Checksum:i94357E45D5F18168
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti402 – 4021Y → N in BAA20530. (PubMed:9172372)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86222 Genomic DNA. Translation: BAA20530.1.
    AP006878 Genomic DNA. Translation: BAD85985.1.
    RefSeqiYP_184209.1. NC_006624.1.

    Genome annotation databases

    EnsemblBacteriaiBAD85985; BAD85985; TK1796.
    GeneIDi3233803.
    KEGGitko:TK1796.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86222 Genomic DNA. Translation: BAA20530.1 .
    AP006878 Genomic DNA. Translation: BAD85985.1 .
    RefSeqi YP_184209.1. NC_006624.1.

    3D structure databases

    ProteinModelPortali O08467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O08467. 1 interaction.
    MINTi MINT-8377176.
    STRINGi 69014.TK1796.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD85985 ; BAD85985 ; TK1796 .
    GeneIDi 3233803.
    KEGGi tko:TK1796.

    Phylogenomic databases

    eggNOGi COG0174.
    HOGENOMi HOG000005156.
    KOi K01915.

    Enzyme and pathway databases

    BioCyci TKOD69014:GH72-1833-MONOMER.

    Family and domain databases

    Gene3Di 3.10.20.70. 1 hit.
    3.30.590.10. 1 hit.
    InterProi IPR008147. Gln_synt_beta.
    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.
    [Graphical view ]
    Pfami PF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54368. SSF54368. 1 hit.
    TIGRFAMsi TIGR00653. GlnA. 1 hit.
    PROSITEi PS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of recombinant glutamine synthetase from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1."
      Adul Rahman R.N.Z., Jongsareejit B., Fujiwara S., Imanaka T.
      Appl. Environ. Microbiol. 63:2472-2476(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, GENE NAME, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.
    2. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
      Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
      Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.

    Entry informationi

    Entry nameiGLNA_THEKO
    AccessioniPrimary (citable) accession number: O08467
    Secondary accession number(s): Q5JJ67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3