ID   GLNA1_VITVI             Reviewed;         356 AA.
AC   P51118;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme 1;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GS1-1; Synonyms=GS1;1;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sultanina; TISSUE=Shoot;
RX   PubMed=8843941; DOI=10.1007/bf00040717;
RA   Loulakakis K.A., Roubelakis-Angelakis K.A.;
RT   "Characterization of Vitis vinifera L. glutamine synthetase and molecular
RT   cloning of cDNAs for the cytosolic enzyme.";
RL   Plant Mol. Biol. 31:983-992(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X94320; CAA63981.1; -; mRNA.
DR   PIR; S71579; S71579.
DR   RefSeq; NP_001268175.1; NM_001281246.1.
DR   AlphaFoldDB; P51118; -.
DR   SMR; P51118; -.
DR   PRIDE; P51118; -.
DR   EnsemblPlants; Vitvi17g00160_t001; Vitvi17g00160_P001; Vitvi17g00160.
DR   GeneID; 100266191; -.
DR   Gramene; Vitvi17g00160_t001; Vitvi17g00160_P001; Vitvi17g00160.
DR   KEGG; vvi:100266191; -.
DR   OMA; HAVACLY; -.
DR   OrthoDB; 784869at2759; -.
DR   ExpressionAtlas; P51118; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   InterPro; IPR008147; Gln_synt_b-grasp.
DR   InterPro; IPR036651; Gln_synt_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..356
FT                   /note="Glutamine synthetase cytosolic isozyme 1"
FT                   /id="PRO_0000153199"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..356
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   356 AA;  39199 MW;  204E675FAC1B790E CRC64;
     MALLSDLINL NLSETTEKVI VEYIWVGGSG MDLRSKARTL SGPVSDPAKL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDTYTPAGE PIPTNKRCNA AKIFSHPDVA
     AEVPWYGIEQ EYTLLQKEVK WPIGWPVGGF PGPQGPYYCG IGADKAWGRD IVDAHYKACL
     YAGINISGIN GEVMPGQWEY QVGPSVGISA GDELWVSRYI LERITEIAGV VLSFDPKPIQ
     GDWNGAGAHT NYSTKSMRND GGFEVIKKAI EKLGLRHKEH IAAYGEGNER RLTGRHETAD
     INTFLWGVAN RGASIRVGRD TEKAGKGYFE DRRPASNMDP YVVTSMIAET TILWKP