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P28786

- GLNA_PROHU

UniProt

P28786 - GLNA_PROHU

Protein

Glutamine synthetase

Gene

glnA

Organism
Proteus hauseri
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      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
    OrganismiProteus hauseri
    Taxonomic identifieri183417 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

    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 – 469469Glutamine synthetasePRO_0000153250Add
    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

    ProteinModelPortaliP28786.
    SMRiP28786. 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.

    P28786-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLEHVLSMI EEHKVRYIDL RFTDTRGKEQ HLTIPAHQVN DDFFEEGKMF    50
    DGSSIGGWKG INESDMVLMP DASTAMLDPF FQDPTLIIRC DVLEPGTMQG 100
    YDRDPRSISK RAEDYLKSSG IADTVLFGPE PEFFLFDDIR FKNDISGASY 150
    AINDIEAAWN TNTKYEDGNK GHRPMVKGGY FPLPPVDSSQ DIRSTMCNIM 200
    EEMGLVVEAH HHEVATAGQN EVATRFNTMT KKADETQIYK YVVQNVAHVF 250
    GKTATFMPKP LVGDNGSGMH CHMSLSKNGT NLFAGDKYGG LSEMALYYIG 300
    GIIKHARALN AFTNPTTNSY KRLVPGFEAP VMLAYSARNR SASIRIPVVA 350
    SMKARRIEVR FPDPLANPYL AFAAQLMAGL DGITNKIHPG DAMDKNLYDL 400
    PPEEAKEIPT VAGSLEEALN ALDADREFLT HGGVFTNDSI DAYLALLRTD 450
    VQRVRMAPHP LEFEMYYSA 469
    Length:469
    Mass (Da):52,205
    Last modified:December 1, 1992 - v1
    Checksum:i852EE660D070E61A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68129 Genomic DNA. Translation: CAA48234.1.
    PIRiS23899.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68129 Genomic DNA. Translation: CAA48234.1 .
    PIRi S23899.

    3D structure databases

    ProteinModelPortali P28786.
    SMRi P28786. Positions 2-468.
    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. "Cloning, heterologous expression, and sequencing of the Proteus vulgaris glnAntrBC operon and implications of nitrogen control on heterologous urease expression."
      Steglitz-Moersdorf U., Moersdorf G., Kaltwasser H.
      FEMS Microbiol. Lett. 106:157-164(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.

    Entry informationi

    Entry nameiGLNA_PROHU
    AccessioniPrimary (citable) accession number: P28786
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 73 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