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P10583

- GLNA_AZOBR

UniProt

P10583 - GLNA_AZOBR

Protein

Glutamine synthetase

Gene

glnA

Organism
Azospirillum brasilense
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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
    OrganismiAzospirillum brasilense
    Taxonomic identifieri192 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

    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 – 468468Glutamine synthetasePRO_0000153229Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei398 – 3981O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP10583.
    SMRiP10583. Positions 7-468.
    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.

    P10583-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDISKVFDL IKEHDVKYVD LRFTDPRGKL HHTAQHVSTI DEDVFEDGIM    50
    FDGSSIAGWK AINESDMILQ LDPTTAVMDP FSAQPTLNIL CDVYEPSTGQ 100
    PYARCPRGIA KAAEKYMASA GIADTAYFGP EAEFFVFDDV KFKVEMNKVS 150
    YEFDSEEGPY TSDKDYEDGN LGHRPGVKGG YFPVAPVDSG SDLRAEMLSV 200
    LAEMGVPVEK HHHEVAASQH ELGIKFDTLV RTGDNMQYYK YVVHNVAHAY 250
    GKTATFMPKP VFGDNGSGMH MHQSIWKEGQ PLFAGNQYAD LSELALYYIG 300
    GIIKHAKALN AFTNPTTNSY KRLVPGYEAP VLLAYSARNR SASCRIPYVA 350
    SPKGKRVEVR FPDPSANPYL AFAALLMAGL DGIQNKIHPG EAMDKNLYDL 400
    PAEELAKVPT VCGSREALDS LKADSAFLQK GDVFTKDMIE SYIDLRTEEL 450
    LAFETMPHPI EYKMYYSV 468
    Length:468
    Mass (Da):51,976
    Last modified:July 1, 1989 - v1
    Checksum:i356AA3803E024F1A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26107 Genomic DNA. Translation: AAA22183.1.
    PIRiA24714. AJKCQB.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26107 Genomic DNA. Translation: AAA22183.1 .
    PIRi A24714. AJKCQB.

    3D structure databases

    ProteinModelPortali P10583.
    SMRi P10583. Positions 7-468.
    ModBasei Search...
    MobiDBi Search...

    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. "Nucleotide sequence of the Azospirillum brasilense Sp7 glutamine synthetase structural gene."
      Bozouklian H., Elmerich C.
      Biochimie 68:1181-1187(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

    Entry informationi

    Entry nameiGLNA_AZOBR
    AccessioniPrimary (citable) accession number: P10583
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 80 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