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Q42624

- GLNAC_BRANA

UniProt

Q42624 - GLNAC_BRANA

Protein

Glutamine synthetase, chloroplastic

Gene

GLN2

Organism
Brassica napus (Rape)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.By similarity

    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, chloroplastic (EC:6.3.1.2)
    Alternative name(s):
    GS2
    Glutamate--ammonia ligase
    Gene namesi
    Name:GLN2
    Synonyms:GLN
    OrganismiBrassica napus (Rape)
    Taxonomic identifieri3708 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

    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 – 4949ChloroplastSequence AnalysisAdd
    BLAST
    Chaini50 – 428379Glutamine synthetase, chloroplasticPRO_0000011175Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Homooctamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ42624.
    SMRiQ42624. Positions 63-411.
    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.

    Q42624-1 [UniParc]FASTAAdd to Basket

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    MAQILAASPT CQMRLTKPSS IASSKLWNSV VLKQKKQSSS KVRSFKVMAL    50
    QSDNSTINRV ESLLNLDTKP FTDRIIAEYI WIGGSGIDLR SKSRTLEKPV 100
    EDPSELPKWN YDGSSTGQAP GEDSEVILYP QAIFRDPFRG GNNILVICDT 150
    YTPAGEPIPT NKRARAAEIF SNKKVNEEIP WFGIEQEYTL LQPNVNWPLG 200
    WPVGAYPGPQ GPYYCGVGAE KSWGRDISDA HYKACLYAGI NISGTNGEVM 250
    PGQWEFQVGP SVGIEAGDHV WCARYLLERI TEQAGVVLTL DPKPIEGDWN 300
    GAGCHTNYST KSMREDGGFE VIKKAILNLS LRHMEHISAY GEGNERRLTG 350
    KHETASIDQF SWGVANRGCS IRVGRDTEKK GKGYLEDRRP ASNMDPYIVT 400
    SLLAETTLLW EPTLEAEALA AQKLSLKV 428
    Length:428
    Mass (Da):47,345
    Last modified:November 1, 1996 - v1
    Checksum:iA0B558C64FD9B18A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501L → I in CAB72423. 1 PublicationCurated
    Sequence conflicti82 – 821I → Y in CAB72423. 1 PublicationCurated
    Sequence conflicti263 – 2631G → R in CAB72423. 1 PublicationCurated
    Sequence conflicti338 – 3381S → I in CAB72423. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72751 mRNA. Translation: CAA51280.1.
    AJ271909 Genomic DNA. Translation: CAB72423.1.
    PIRiS32228.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72751 mRNA. Translation: CAA51280.1 .
    AJ271909 Genomic DNA. Translation: CAB72423.1 .
    PIRi S32228.

    3D structure databases

    ProteinModelPortali Q42624.
    SMRi Q42624. Positions 63-411.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Chloroplastic glutamine synthetase from Brassica napus."
      Ochs G., Schock G., Wild A.
      Plant Physiol. 103:303-304(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    2. "Cloning and Sequencing of genomic fragments coding for glutamine synthetase of Brassica napus."
      Wojtyna S., Ochs G., Wild A.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Drakkar.
      Tissue: Leaf.

    Entry informationi

    Entry nameiGLNAC_BRANA
    AccessioniPrimary (citable) accession number: Q42624
    Secondary accession number(s): Q9M429
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3