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P08281

- GLNA2_PEA

UniProt

P08281 - GLNA2_PEA

Protein

Glutamine synthetase leaf isozyme, chloroplastic

Gene

GS2

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      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
    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 leaf isozyme, chloroplastic (EC:6.3.1.2)
    Alternative name(s):
    GS2
    Glutamate--ammonia ligase
    Gene namesi
    Name:GS2
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    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 – 4949ChloroplastAdd
    BLAST
    Chaini50 – 430381Glutamine synthetase leaf isozyme, chloroplasticPRO_0000011182Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.

    Structurei

    3D structure databases

    ProteinModelPortaliP08281.
    SMRiP08281. Positions 64-413.
    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.

    P08281-1 [UniParc]FASTAAdd to Basket

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    MAQILAPSTQ WQMRITKTSP CATPITSKMW SSLVMKQTKK VAHSAKFRVM    50
    AVNSENGTIN RVEDLLNLDI TPFTDSIIAE YIWIGGTGID VRSKSRTISK 100
    PVSHPSEVPK WNYDGSSTGQ APGEDSEVIL YPQAIFKDPF RGGNNILVVC 150
    DAYTPAGEPI PTNKRHRAAE IFSNPKVEAE IPWYGIEQEY TLLQTNVKWP 200
    LGWPVGGYPG PQGPYYCAAG ADKSFGRDIS DAHYKACIYA GINISGTNGE 250
    VMPGQWEYQV GPSVGIEAGD HIWASRYILE RITEQAGVVL TLDPKPIEGD 300
    WNGAGCHTNY STKSMREDGG FEVIKKAILN LSLRHKIHIE AYGEGNERRL 350
    TGKHETASIN DFSWGVANRG CSIRVGRDTE KNGKGYLEDR RPASNMDPYV 400
    VTALLAESTL LWEPTLEAEA LAAQKIALKV 430
    Length:430
    Mass (Da):47,346
    Last modified:July 1, 1989 - v2
    Checksum:iAB7EFA4F53970D7E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20664 mRNA. Translation: AAA33653.1.
    X05514 mRNA. Translation: CAA29057.1.
    PIRiA28089. AJPMQ2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20664 mRNA. Translation: AAA33653.1 .
    X05514 mRNA. Translation: CAA29057.1 .
    PIRi A28089. AJPMQ2.

    3D structure databases

    ProteinModelPortali P08281.
    SMRi P08281. Positions 64-413.
    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. "Chloroplast and cytosolic glutamine synthetase are encoded by homologous nuclear genes which are differentially expressed in vivo."
      Tingey S.V., Tsai F., Edwards J., Walker E.L., Coruzzi G.M.
      J. Biol. Chem. 263:9651-9657(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Glutamine synthetase genes of pea encode distinct polypeptides which are differentially expressed in leaves, roots and nodules."
      Tingey S.V., Walker E.L., Coruzzi G.M.
      EMBO J. 6:1-9(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-430.
      Strain: cv. Sparkle.

    Entry informationi

    Entry nameiGLNA2_PEA
    AccessioniPrimary (citable) accession number: P08281
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 81 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In pea there are distinct isozymes in leaves, roots and nodules.
    Irreversibly inhibited by the herbicide L-phosphinothricin (PPT).

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3