ID   GLNA3_HORVU             Reviewed;         356 AA.
AC   Q06378;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Cytoplasmic GS3;
DE   AltName: Full=Glutamate--ammonia ligase;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8104170; DOI=10.1111/j.1601-5223.1993.00281.x;
RA   Marigo C., Zito F., Casadoro G.;
RT   "Isolation and characterization of a cDNA coding for cytoplasmic glutamine
RT   synthetase of barley.";
RL   Hereditas 118:281-284(1993).
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   -!- MISCELLANEOUS: In barley, there are distinct isozymes in the
CC       chloroplast, and cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X69087; CAA48830.1; -; mRNA.
DR   AlphaFoldDB; Q06378; -.
DR   SMR; Q06378; -.
DR   PRIDE; Q06378; -.
DR   SABIO-RK; Q06378; -.
DR   ExpressionAtlas; Q06378; 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"
FT                   /id="PRO_0000153173"
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;  39128 MW;  541DB976BFF04BC5 CRC64;
     MALLTDLLNL DLSGSTEKII AEYIWIGGSG MDLRSKARHL PGPVTHPSKL PKWNYDGSST
     GQAPGEDSEV ILYPQAILKD PFREGNNILV MCDCYTPRGE PIPTNKRYNA AKILSNPDVA
     KEEPWYGIEQ EYTLLQKDIN WPLGWPVGGF PGPQGPYYCG IGADKSFGRD IVDSHYKACL
     FGGVNISGIN GEVMPGQWEF QVGPTVGISA GDQVWVARYI LERITEIAGV VVTFDPKPIP
     GDWNGAGAHT NYSTESMRND GGFKVIVDAV EKLKLKHKEH IAAYGEGNER RLTGKHETAD
     INTSSWGVAN RGASVRVGRE TEQNGKGYFE DRRPASNMDP YVVTSMIAQT TILWKP