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P33035

- GLNA_MICDP

UniProt

P33035 - GLNA_MICDP

Protein

Glutamine synthetase

Gene

glnA

Organism
Microchaete diplosiphon (Fremyella diplosiphon)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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
    OrganismiMicrochaete diplosiphon (Fremyella diplosiphon)
    Taxonomic identifieri1197 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaNostocalesMicrochaetaceaeMicrochaete

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 471470Glutamine synthetasePRO_0000153216Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei399 – 3991O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP33035.
    SMRiP33035. Positions 2-470.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P33035-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTPQEVLKL IQDQKIQMID LKFIDTPGTW QHLTVYYNQI DESSFTDGVP    50
    FDGSSIRGWK GIEESDMTMV LDPNTAWIDP FMKEPTLSII CSIKEPRTGE 100
    WYNRCPRVIA QKAIDYLVST GLGDTAFFGP EAEFFIFDDA RFDQTANSGY 150
    YYVDSVEGRW NSGKDEGPNL AYKPRFKEGY FPVAPTDTFQ DMRTEMLLTM 200
    AACGVPIEKQ HHEVATGGQC ELGFRFGKLI EAADWLMTYK YVIKNVAKKY 250
    GRTVTFMPKP IFGDNGSGMH CHQSIWKDGK PLFGGDKYAG LSDMALYYIG 300
    GILKHAPALL GITNPTTNSY KRLVPGYEAP VNLAYSQGNR SASVRIPLSG 350
    TNPKAKRLEF RCPDATSNPY LAFAAMLCAG IDGIKNKIHP GEPLDRNIYE 400
    LSPEELAKVP STPGSLELAL EALENDHAFL TESGVFTEDF IQNWIEYKLV 450
    NEVKQLQLRP HPYEFYLYYD C 471
    Length:471
    Mass (Da):53,050
    Last modified:January 23, 2007 - v2
    Checksum:i4216D115B6EC7310
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05609 Genomic DNA. Translation: AAA23288.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05609 Genomic DNA. Translation: AAA23288.1 .

    3D structure databases

    ProteinModelPortali P33035.
    SMRi P33035. Positions 2-470.
    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. "Molecular characterization of the gene encoding glutamine synthetase in the cyanobacterium Calothrix sp. PCC 7601."
      Elmorjani K., Liotenberg S., Houmard J., de Marsac N.T.
      Biochem. Biophys. Res. Commun. 189:1296-1302(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGLNA_MICDP
    AccessioniPrimary (citable) accession number: P33035
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 72 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