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P07804

- GLNA_ACIFR

UniProt

P07804 - GLNA_ACIFR

Protein

Glutamine synthetase

Gene

glnA

Organism
Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Alternative name(s):
    Glutamate--ammonia ligase
    Gene namesi
    Name:glnA
    OrganismiAcidithiobacillus ferrooxidans (Thiobacillus ferrooxidans)
    Taxonomic identifieri920 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

    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_0000153274Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei397 – 3971O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP07804.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP07804.
    SMRiP07804. Positions 4-468.
    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.

    P07804-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGYSPSDVVK LIQEKDIKFI DFRFTDTKGK EQHVSVPGHV IEEDTFTEGK    50
    AFDGSSIAGW KGINESDMIL LPDPDSAVLD PFMDETTLLL RCDVIEPATG 100
    QGYERDPRSV AKRAEIYLKS TGIADTSFFG PEFFVFDSVT WNIDMSGCAY 150
    KVDAEEAAWN SGKEYESGNM GHRLGVKGGY FPVPPVDSAQ DLRSAMCLAM 200
    EEMGLKVEVH HHEVATAGQH EIGVGFNTLT PRRMRCKILK YVVHNVAAVR 250
    QTATFMPKPV VGDNGSGMHV HQSLGKDGKN IFAGDLYGGL SEIALYYIGG 300
    IIKHAKAVNA LTNPSTNSYK RLVPHFEAPV LLAYSAKNRS ASIRIPYVNS 350
    PKARRIEVRF PDSTANPYLA FSAMLMAGLD GIQNKIHPAT AMDKNLYDLP 400
    AEEQANIPGV AASLEEALRA LEADHDFLMK GGVFSESWLE GYLDVKWAEV 450
    QTLRVTTHPV EFQMYYSL 468
    Length:468
    Mass (Da):51,614
    Last modified:August 1, 1988 - v1
    Checksum:i24710B272B3A7054
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16626 Genomic DNA. Translation: AAA27370.1.
    PIRiA29460. AJBCQF.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16626 Genomic DNA. Translation: AAA27370.1 .
    PIRi A29460. AJBCQF.

    3D structure databases

    ProteinModelPortali P07804.
    SMRi P07804. Positions 4-468.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P07804.

    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 glutamine synthetase gene and its controlling region from the acidophilic autotroph Thiobacillus ferrooxidans."
      Rawlings D.E., Jones W.A., O'Neill E.G., Woods D.R.
      Gene 53:211-217(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGLNA_ACIFR
    AccessioniPrimary (citable) accession number: P07804
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 77 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