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P43518

- GLNA_RHOSH

UniProt

P43518 - GLNA_RHOSH

Protein

Glutamine synthetase

Gene

glnA

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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)
    Short name:
    GS
    Alternative name(s):
    Glutamate--ammonia ligase
    Gene namesi
    Name:glnA
    OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
    Taxonomic identifieri1063 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

    Subcellular locationi

    Cytoplasm By similarity

    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_0000153256Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP43518.
    SMRiP43518. Positions 5-466.
    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.
    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.

    P43518-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKVADALKL MKDEEVEYVD IRFTDPRGKL QHVTLVADLV DEDFFEEGFM    50
    FDGSSIAGWK SIDQSDMKLI PDAGSVYIDP FYAEKTLCVH CNVVEPDTGE 100
    AYSRDPRGAA VKAEAYLKAS GIGDVAYFGP EAEFFIFDDV RYSVTPAKVA 150
    YQIDADAGAW NTDSEYEMGN LAHRAGHKGG YFPVNPIDEA QDLRGEMLST 200
    MKRMGMKVDK HHHEVATCQH ELGLIFGGLT EQADNILKYK YVIHNVAGMH 250
    GKTVTFMPKP MKGDNGSGMH VNMSIWKEQA LFAGDKYADL SQEALWFIGG 300
    ILKQPSVNAL TNPATNSYKR LIPGFEAPVL RAYSARNRSG CVRIPWTESP 350
    NAKRVEARFP DPSANPYLAF AALLMAGLDG IKNKIDPGPA SDKDLYDLPP 400
    EELAAIPTVC GSLREALEEL EKDHDFLLAG DVFTKDQLEG YMALKWEEVY 450
    AYEHTPHPVE YQMYYSC 467
    Length:467
    Mass (Da):51,964
    Last modified:November 1, 1995 - v1
    Checksum:iBA93A04250BFB978
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71659 Genomic DNA. Translation: CAA50651.1.
    PIRiS33181.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71659 Genomic DNA. Translation: CAA50651.1 .
    PIRi S33181.

    3D structure databases

    ProteinModelPortali P43518.
    SMRi P43518. Positions 5-466.
    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.
    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. "Nucleotide sequence and characterization of the Rhodobacter sphaeroides glnB and glnA genes."
      Zinchenko V.V., Churin Y., Shestopalov V.I., Shestakov S.V.
      Microbiology 140:2143-2151(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 2R.

    Entry informationi

    Entry nameiGLNA_RHOSH
    AccessioniPrimary (citable) accession number: P43518
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 65 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