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 27-MAR-2024, entry version 98.
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 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:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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 PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF93; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-4; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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
//
