ID   GLNA1_MEDSA             Reviewed;         356 AA.
AC   P04078;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tischer E., Dassarma S., Goodman H.M.;
RT   "Nucleotide sequence of an alfalfa glutamine synthetase gene.";
RL   Mol. Gen. Genet. 203:221-229(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 266-356.
RX   PubMed=6152283;
RA   Donn G., Tischer E., Smith J.A., Goodman H.M.;
RT   "Herbicide-resistant alfalfa cells: an example of gene amplification in
RT   plants.";
RL   J. Mol. Appl. Genet. 2:621-635(1984).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
CC       phosphinothricin (PPT).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; K03282; AAA32654.1; -; mRNA.
DR   EMBL; X03931; CAA27570.1; -; Genomic_DNA.
DR   PIR; A26025; AJAAQ.
DR   AlphaFoldDB; P04078; -.
DR   SMR; P04078; -.
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; Nitrogen fixation; Nucleotide-binding.
FT   CHAIN           1..356
FT                   /note="Glutamine synthetase cytosolic isozyme"
FT                   /id="PRO_0000153183"
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"
FT   REGION          38..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  39107 MW;  B4450F5489B27BD7 CRC64;
     MSLLSDLINL DLSETTEKII AEYIWIGGSG LDLRSKARTL PGPVTDPSQL PKWNYDGSST
     GQAPGEDSEV IIYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AKIFSHPDVV
     AEVPWYGIEQ EYTLLQKDIN WPLGWPVGGF PGPQGPYYCG AGADKAFGRD IVDSHYKACL
     YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWVARYI LERITEVAGV VLSFDPKPIK
     GDWNGAGAHT NYSTKSMRED GGYEVILKAI EKLGKKHKEH IAAYGEGNER RLTGRHETAD
     INTFLWGVAN RGASIRVGRD TEKAGKGYFE DRRPSSNMDP YVVTSMIADT TILWKP