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P13564

- GLNA2_HORVU

UniProt

P13564 - GLNA2_HORVU

Protein

Glutamine synthetase leaf isozyme, chloroplastic

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    The light-modulated chloroplast enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration.

    Catalytic activityi

    ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

    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

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase leaf isozyme, chloroplastic (EC:6.3.1.2)
    Alternative name(s):
    GS2
    Glutamate--ammonia ligase
    OrganismiHordeum vulgare (Barley)
    Taxonomic identifieri4513 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

    Organism-specific databases

    GrameneiP13564.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5454ChloroplastAdd
    BLAST
    Chaini55 – 434380Glutamine synthetase leaf isozyme, chloroplasticPRO_0000011178Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP13564.

    Interactioni

    Subunit structurei

    Homooctamer.

    Structurei

    3D structure databases

    ProteinModelPortaliP13564.
    SMRiP13564. Positions 66-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.30.590.10. 1 hit.
    InterProiIPR008147. Gln_synt_beta.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    IPR008146. Gln_synth_cat_dom.
    IPR027303. Gln_synth_gly_rich_site.
    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.
    PROSITEiPS00180. GLNA_1. 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.

    P13564-1 [UniParc]FASTAAdd to Basket

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    MQVRRDDDGA GGCAGDAVPG GGEGQDGVPA RQPAGRVWGV SRAARATSGF    50
    KVLALGPETT GVIQRMQQLL DMDTTPFTDK IIAEYIWVGG SGIDLRSKSR 100
    TISKPVEDPS ELPKWNYDGS STGQAPGEDS EVILYPQAIF KDPFRGGNNI 150
    LVICDTYTPQ GEPIPTNKRH MAAQIFSDPK VTSQVPWFGI EQEYTLMQRD 200
    VNWPLGWPVG GYPGPQGPYY CAVGSDKSFG RDISDAHYKA CLYAGIEISG 250
    TNGEVMPGQW EYQVGPSVGI DAGDHIWASR YILERITEQA GVVLTLDPKP 300
    IQGDWNGAGC HTNYSTLSMR EDGGFDVIKK AILNLSLRHD LHIAAYGEGN 350
    ERRLTGLHET ASISDFSWGV ANRGCSIRVG RDTEAKGKGY LEDRRPASNM 400
    DPYTVTALLA ETTILWEPTL EAEALAAKKL ALKV 434
    Length:434
    Mass (Da):47,094
    Last modified:November 1, 1990 - v2
    Checksum:iFC47F5685EFC0D1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 2719GAGGC…EGQDG → AQAVVQAMQCQVGVRGRTA in CAA34131. (PubMed:1983286)CuratedAdd
    BLAST
    Sequence conflicti41 – 411S → R in CAA34131. (PubMed:1983286)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53580 mRNA. Translation: CAA37643.1.
    X16000 mRNA. Translation: CAA34131.1.
    PIRiS11865. AJBHQ.
    UniGeneiHv.733.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53580 mRNA. Translation: CAA37643.1 .
    X16000 mRNA. Translation: CAA34131.1 .
    PIRi S11865. AJBHQ.
    UniGenei Hv.733.

    3D structure databases

    ProteinModelPortali P13564.
    SMRi P13564. Positions 66-417.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P13564.

    Gene expression databases

    Genevestigatori P13564.

    Family and domain databases

    Gene3Di 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.
    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.
    PROSITEi PS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cDNA sequence coding for glutamine synthetase in Hordeum vulgare L."
      Stroman P., Baima S., Casadoro G.
      Plant Mol. Biol. 15:161-163(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular analysis of barley mutants deficient in chloroplast glutamine synthetase."
      Freeman J., Marquez A.J., Wallsgrove R.M., Saarelainen R., Forde B.G.
      Plant Mol. Biol. 14:297-311(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-434.
      Strain: cv. Maris Mink.
      Tissue: Leaf.
    3. "Characterization of a cDNA clone for barley leaf glutamine synthetase."
      Baima S., Haegi A., Stroman P., Casadoro G.
      Carlsberg Res. Commun. 54:1-9(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-434.

    Entry informationi

    Entry nameiGLNA2_HORVU
    AccessioniPrimary (citable) accession number: P13564
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In barley, there are distinct isozymes in the chloroplast, and cytoplasm.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3