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P13499

- GLNA_RHOCA

UniProt

P13499 - GLNA_RHOCA

Protein

Glutamine synthetase

Gene

glnA

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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
    OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
    Taxonomic identifieri1061 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

    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 – ›438›438Glutamine synthetasePRO_0000153255Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP13499.
    SMRiP13499. Positions 3-437.
    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: Fragment.

    P13499-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAVKKALDL MKAEEVEYVD IRFCDPRGKL QHVTLIADLV DEDFFEEGFM    50
    FDGSSIAGWK SIDQSDMKLI PDASSVYIDP FYAEKTMCVH CNVVEPDTAE 100
    AYSRDPRIAL KAEAYLKASG IGDVAYFGPE AEFFIFDDVR YSVTPAKVAY 150
    QIDAEAAAWN TDAEVEMGNL AHRAGHKGGY FPVNPVDEAQ DLRGEMLSTM 200
    KRMGMKVDKH HHEVATCQHE LGLIFGGLTE QADNILKYKY VIHNVAHAYG 250
    KTVTFMPKPM KGDNGSGMHV NMSIWKDGKP LFAGDKYADL SQEALYFIGG 300
    ILKHAKALNA LTNPGTNSYK RLIPGFEAPV LRAYSARNRS GCVRIPWTES 350
    PKAKRVEARF PDPSANPYLA FAALLMAGLD GIKNKIDPGP ASDKDLYDLP 400
    PEELAAIPTV CGSLREALTE LEKDHDFLLA GDVFTKDQ 438
    Length:438
    Mass (Da):48,391
    Last modified:October 1, 1996 - v2
    Checksum:i07B81EBF6534991F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei438 – 4381

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25953 Genomic DNA. Translation: AAA87025.1.
    M28244 Genomic DNA. Translation: AAA26123.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25953 Genomic DNA. Translation: AAA87025.1 .
    M28244 Genomic DNA. Translation: AAA26123.1 .

    3D structure databases

    ProteinModelPortali P13499.
    SMRi P13499. Positions 3-437.
    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. "Inactivation, sequence, and lacZ fusion analysis of a regulatory locus required for repression of nitrogen fixation genes in Rhodobacter capsulatus."
      Kranz R.G., Pace V.M., Caldicott I.M.
      J. Bacteriol. 172:53-62(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
    2. "Regulation of the glnBA operon of Rhodobacter capsulatus."
      Borghese R., Wall J.D.
      J. Bacteriol. 177:4549-4552(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-438.
      Strain: ATCC 33303 / B10.

    Entry informationi

    Entry nameiGLNA_RHOCA
    AccessioniPrimary (citable) accession number: P13499
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 78 of the entry and version 2 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