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P19904

- GLNA_VIBAL

UniProt

P19904 - GLNA_VIBAL

Protein

Glutamine synthetase

Gene

glnA

Organism
Vibrio alginolyticus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Feb 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: 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
    OrganismiVibrio alginolyticus
    Taxonomic identifieri663 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

    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_0000153275Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP19904.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP19904.
    SMRiP19904. Positions 2-468.
    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.

    P19904-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVEKVLSLI QENEVKFVDL RFTDTKGKEQ HISIPAHQID ADFFEEGKMF    50
    DGSSVAGWKG INESDMVMMP DASSAVLDPF TEDATLNIRC DILEPATMQG 100
    YDRDPRSIAK RAEDFMRSTG VADTVLIGPE PEFFLFDDVK FATDMSGSFF 150
    KIDDVEAAWN TGSDYEEGNK GHRPGVKGGY FPVAPVDSSQ DIRSAMCLVM 200
    EEMGLVVEAH HHEATAGQNE IATRFNTLTT KADEIQIYKY VVHNVAHAFG 250
    KTATFMPKPL VGDNGSGMHV HQSLAKDGVN LFAGDKYGGL SEMALYYIGG 300
    IIKHARAINA FANPSTNSYK RLVPGFEAPV MLAYSARNRS ASIRIPVVPS 350
    PKARRIEVRF GDPAANPYLC FASMLMAGLD GIKNKIHPGE AMDKDLYDLP 400
    AEESAEIPTV AYSLKDALAE LDADREFLTA GGVFSDDFID SYIELKSQDV 450
    ERVNMTTHPV EFELYYSV 468
    Length:468
    Mass (Da):51,556
    Last modified:February 1, 1991 - v1
    Checksum:iABB66AA9C072D856
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08499 Genomic DNA. Translation: AAA27523.1.
    PIRiJL0113. AJVCQA.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08499 Genomic DNA. Translation: AAA27523.1 .
    PIRi JL0113. AJVCQA.

    3D structure databases

    ProteinModelPortali P19904.
    SMRi P19904. Positions 2-468.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P19904.

    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 Vibrio alginolyticus glnA region."
      Maharaj R., Rumbak E., Jones W.A., Robb S.M., Robb F.T., Woods D.R.
      Arch. Microbiol. 152:542-549(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGLNA_VIBAL
    AccessioniPrimary (citable) accession number: P19904
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 74 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