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P22248

- GLNA_AZOVI

UniProt

P22248 - GLNA_AZOVI

Protein

Glutamine synthetase

Gene

glnA

Organism
Azotobacter vinelandii
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      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: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Nitrogen fixation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Alternative name(s):
    Glutamate--ammonia ligase
    Gene namesi
    Name:glnA
    OrganismiAzotobacter vinelandii
    Taxonomic identifieri354 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

    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 – 467467Glutamine synthetasePRO_0000153231Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei396 – 3961O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP22248.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP22248.
    SMRiP22248. Positions 5-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    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.
    IPR001637. Gln_synth_I_adenylation_site.
    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.
    PS00182. GLNA_ADENYLATION. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22248-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKSLQLIKE HDVKWIDLRF TDTKGKQQHV TMPARDVDDD FFEYGKMFDG    50
    SSIAGWKGIE ASDMILMPDD STAVLDPFTE EPTLIIVCDI IEPSTMQGYD 100
    RDPRAIARRA EEYLKSTGIG DTAFFGPEPE FFIFDEVKYK SDISGSMFKI 150
    FSEQAAWNTD ADFEGGNKGH RPGVKGGYFP VPPVDHDHEI RTAMCNALEE 200
    MGLKVEVHHH EVATAGQNEI GVSFNTLVAK ADEVQTLKYC VHNVADAYGK 250
    TVTFMPKPLY GDNGSGMHVH MSIAKDGKNT FAGEGYAGLS DTALYFIGGI 300
    IKHGKALNGF TNPSTNSYKR LVPGFEAPVM LAYSARNRSA SIRIPYVNSP 350
    KARRIEARFP DPSANPYLAF AALLMAGLDG IQNKIHPGDA ADKNLYDLPP 400
    EEAKEIPQVC GSLKEALEEL DKGRAFLTKG GVFSDDFIDA YLELKSEEEI 450
    KVRTFVHPLE YDLYYSV 467
    Length:467
    Mass (Da):51,746
    Last modified:August 1, 1991 - v1
    Checksum:iD4EFA6EC895E38AF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57275 Genomic DNA. Translation: AAA62673.1.
    PIRiA37153. AJAVQ.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57275 Genomic DNA. Translation: AAA62673.1 .
    PIRi A37153. AJAVQ.

    3D structure databases

    ProteinModelPortali P22248.
    SMRi P22248. Positions 5-467.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P22248.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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.
    IPR001637. Gln_synth_I_adenylation_site.
    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.
    PS00182. GLNA_ADENYLATION. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular analysis of the Azotobacter vinelandii glnA gene encoding glutamine synthetase."
      Toukdarian A., Saunders G., Selman-Sosa G., Santero E., Woodley P., Kennedy C.
      J. Bacteriol. 172:6529-6539(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGLNA_AZOVI
    AccessioniPrimary (citable) accession number: P22248
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3