ID   GLNA2_VITVI             Reviewed;         356 AA.
AC   P51119;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme 2;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GS1-2; Synonyms=GS1;2;
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; X94321; CAA63982.1; -; mRNA.
DR   PIR; S71580; S71580.
DR   RefSeq; NP_001268054.1; NM_001281125.1.
DR   AlphaFoldDB; P51119; -.
DR   SMR; P51119; -.
DR   STRING; 29760.VIT_14s0006g00350.t01; -.
DR   PRIDE; P51119; -.
DR   GeneID; 100246404; -.
DR   KEGG; vvi:100246404; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   OrthoDB; 784869at2759; -.
DR   ExpressionAtlas; P51119; 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 2"
FT                   /id="PRO_0000153200"
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;  39322 MW;  5EB0D289F971E5D7 CRC64;
     MALLSDLINL NLSDVTEKII AEYIWIGGSG MDLRSKARTL SGPVSDPHKL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDTYTPAGE PIPTNKRHNA AKIFSHPEVL
     AEETWYGIEQ EYTLLQNSVK WPIGWPVGGY PGPQGPYYCG IGADKAFGRD IVDSHYKACL
     YAGINISGIN GEVMPGQWEF QVGPAVGISA GDELWVARYI LERITEIAGV VVSFDPKPIQ
     GDWNGAGAHT NYSTKSMRND GGYEIIKKAI EKLGLRHKEH IAAYGEGNER RLTGRHETAD
     INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAES TILWKP