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P99095

- GLNA_STAAN

UniProt

P99095 - GLNA_STAAN

Protein

Glutamine synthetase

Gene

glnA

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    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

    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

    BioCyciSAUR158879:GJCB-1211-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:SA1150
    OrganismiStaphylococcus aureus (strain N315)
    Taxonomic identifieri158879 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000751: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446Glutamine synthetasePRO_0000153259Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei375 – 3751O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP99095.

    2D gel databases

    SWISS-2DPAGEP99095.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi158879.SA1150.

    Structurei

    3D structure databases

    ProteinModelPortaliP99095.
    SMRiP99095. Positions 7-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0174.
    HOGENOMiHOG000005156.
    KOiK01915.
    OMAiIEWDMFR.
    OrthoDBiEOG6B360N.

    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.

    P99095-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRTFTKED IRKFAEEENV RYLRLQFTDI LGTIKNVEVP VSQLEKVLDN    50
    EMMFDGSSIE GFVRIEESDM YLHPDLDTWV IFPWTAGQGK VARLICDVYK 100
    TDGTPFEGDP RANLKRVLKE MEDLGFTDFN LGPEPEFFLF KLDEKGEPTL 150
    ELNDDGGYFD LAPTDLGENC RRDIVLELED MGFDIEASHH EVAPGQHEID 200
    FKYADAVTAC DNIQTFKLVV KTIARKHNLH ATFMPKPLFG VNGSGMHFNV 250
    SLFKGKENAF FDPNTEMGLT ETAYQFTAGV LKNARGFTAV CNPLVNSYKR 300
    LVPGYEAPCY IAWSGKNRSP LIRVPSSRGL STRIEVRSVD PAANPYMALA 350
    AILEAGLDGI KNKLKVPEPV NQNIYEMNRE EREAVGIQDL PSTLYTALKA 400
    MRENEVIKKA LGNHIYNQFI NSKSIEWDYY RTQVSEWERD QYMKQY 446
    Length:446
    Mass (Da):50,855
    Last modified:April 13, 2004 - v1
    Checksum:iFF9F25631167903D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42404.1.
    PIRiH89905.
    RefSeqiNP_374425.1. NC_002745.2.

    Genome annotation databases

    EnsemblBacteriaiBAB42404; BAB42404; BAB42404.
    GeneIDi1123983.
    KEGGisau:SA1150.
    PATRICi19574524. VBIStaAur116463_1231.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42404.1 .
    PIRi H89905.
    RefSeqi NP_374425.1. NC_002745.2.

    3D structure databases

    ProteinModelPortali P99095.
    SMRi P99095. Positions 7-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158879.SA1150.

    2D gel databases

    SWISS-2DPAGE P99095.

    Proteomic databases

    PRIDEi P99095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB42404 ; BAB42404 ; BAB42404 .
    GeneIDi 1123983.
    KEGGi sau:SA1150.
    PATRICi 19574524. VBIStaAur116463_1231.

    Phylogenomic databases

    eggNOGi COG0174.
    HOGENOMi HOG000005156.
    KOi K01915.
    OMAi IEWDMFR.
    OrthoDBi EOG6B360N.

    Enzyme and pathway databases

    BioCyci SAUR158879:GJCB-1211-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: N315.
    2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: N315.
    3. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
      Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
      Submitted (OCT-2007) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: N315.

    Entry informationi

    Entry nameiGLNA_STAAN
    AccessioniPrimary (citable) accession number: P99095
    Secondary accession number(s): Q99UG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3