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P20477

- GLNA1_DROME

UniProt

P20477 - GLNA1_DROME

Protein

Glutamine synthetase 1, mitochondrial

Gene

Gs1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    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: FlyBase

    GO - Biological processi

    1. glutamine biosynthetic process Source: InterPro
    2. glutamine metabolic process Source: FlyBase
    3. mitochondrion organization Source: FlyBase

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_202933. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
    REACT_216833. Amino acid synthesis and interconversion (transamination).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase 1, mitochondrial (EC:6.3.1.2)
    Alternative name(s):
    Glutamate--ammonia ligase 1
    Gene namesi
    Name:Gs1
    ORF Names:CG2718
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0001142. Gs1.

    Subcellular locationi

    GO - Cellular componenti

    1. lipid particle Source: FlyBase
    2. mitochondrion Source: FlyBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
    BLAST
    Chaini28 – 399372Glutamine synthetase 1, mitochondrialPRO_0000011173Add
    BLAST

    Proteomic databases

    PaxDbiP20477.

    Expressioni

    Gene expression databases

    BgeeiP20477.

    Interactioni

    Subunit structurei

    Homooctamer.

    Protein-protein interaction databases

    BioGridi59433. 20 interactions.
    MINTiMINT-297766.

    Structurei

    3D structure databases

    ProteinModelPortaliP20477.
    SMRiP20477. Positions 45-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0174.
    GeneTreeiENSGT00390000010047.
    HOGENOMiHOG000246596.
    InParanoidiP20477.
    KOiK01915.
    OMAiKSFGRDV.
    OrthoDBiEOG7CZK5G.
    PhylomeDBiP20477.

    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.

    P20477-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALRVAGLFL KKELVAPATQ QLRLLRTGNT TRSQFLANSP NTALDKSILQ    50
    RYRNLETPAN RVQATYLWID GTGENIRLKD RVLDKVPSSV EDLPDWQYDG 100
    SSTYQAHGEN SDTTLKPRAI YRDPFKPGKN DVIVLCDTYS ADGKPTASNK 150
    RAAFQAAIDL ISDQEPWFGI EQEYTLLDVD GRPFGWPENG FPAPQGPYYC 200
    GVGADRVYAR DLVEAHVVAC LYAGIDFAGT NAEVMPAQWE FQIGPAGIKA 250
    CDDLWVSRYI LQRIAEEYGV VVTFDPKPME GQWNGAGAHT NFSTKEMRAD 300
    GGIKAIEEAI EKLSKRHERH IKAYDPKEGK DNERRLVGRL ETSSIDKFSW 350
    GVANRAVSVR VPRGVATAGK GYLEDRRPSS NCDPYAVCNA IVRTCLLNE 399
    Length:399
    Mass (Da):44,396
    Last modified:June 21, 2005 - v3
    Checksum:i935E8D1D9927ACCC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → R in CAA10031. 1 PublicationCurated
    Sequence conflicti178 – 1836DVDGRP → RRGRTS in CAA36971. (PubMed:1969491)Curated
    Sequence conflicti288 – 2881A → R in CAA36971. (PubMed:1969491)Curated
    Sequence conflicti309 – 3091A → P in CAA36971. (PubMed:1969491)Curated
    Sequence conflicti325 – 3251D → Y in CAA36971. (PubMed:1969491)Curated
    Sequence conflicti393 – 3931R → Q in CAA36971. (PubMed:1969491)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52760 mRNA. Translation: CAA36971.1.
    AJ012460 mRNA. Translation: CAA10031.1.
    AE014134 Genomic DNA. Translation: AAF51546.1.
    AE014134 Genomic DNA. Translation: AAF51547.1.
    AY058730 mRNA. Translation: AAL13959.1.
    PIRiS09109. AJFF1M.
    RefSeqiNP_001162839.1. NM_001169368.2.
    NP_476570.1. NM_057222.3.
    NP_722606.1. NM_164367.1.
    UniGeneiDm.6999.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078114; FBpp0077773; FBgn0001142.
    FBtr0078115; FBpp0077774; FBgn0001142.
    FBtr0300568; FBpp0289795; FBgn0001142.
    GeneIDi33172.
    KEGGidme:Dmel_CG2718.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52760 mRNA. Translation: CAA36971.1 .
    AJ012460 mRNA. Translation: CAA10031.1 .
    AE014134 Genomic DNA. Translation: AAF51546.1 .
    AE014134 Genomic DNA. Translation: AAF51547.1 .
    AY058730 mRNA. Translation: AAL13959.1 .
    PIRi S09109. AJFF1M.
    RefSeqi NP_001162839.1. NM_001169368.2.
    NP_476570.1. NM_057222.3.
    NP_722606.1. NM_164367.1.
    UniGenei Dm.6999.

    3D structure databases

    ProteinModelPortali P20477.
    SMRi P20477. Positions 45-399.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59433. 20 interactions.
    MINTi MINT-297766.

    Proteomic databases

    PaxDbi P20477.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078114 ; FBpp0077773 ; FBgn0001142 .
    FBtr0078115 ; FBpp0077774 ; FBgn0001142 .
    FBtr0300568 ; FBpp0289795 ; FBgn0001142 .
    GeneIDi 33172.
    KEGGi dme:Dmel_CG2718.

    Organism-specific databases

    CTDi 33172.
    FlyBasei FBgn0001142. Gs1.

    Phylogenomic databases

    eggNOGi COG0174.
    GeneTreei ENSGT00390000010047.
    HOGENOMi HOG000246596.
    InParanoidi P20477.
    KOi K01915.
    OMAi KSFGRDV.
    OrthoDBi EOG7CZK5G.
    PhylomeDBi P20477.

    Enzyme and pathway databases

    Reactomei REACT_202933. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
    REACT_216833. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    GenomeRNAii 33172.
    NextBioi 782262.

    Gene expression databases

    Bgeei P20477.

    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. "Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster."
      Caizzi R., Bozzetti M.P., Caggese C., Ritossa F.
      J. Mol. Biol. 212:17-26(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Glover D.M.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiGLNA1_DROME
    AccessioniPrimary (citable) accession number: P20477
    Secondary accession number(s): A4UZX3, O96770, Q9VPK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3