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Database: UniProt
Entry: W1NJA2_AMBTC
LinkDB: W1NJA2_AMBTC
Original site: W1NJA2_AMBTC 
ID   W1NJA2_AMBTC            Unreviewed;       356 AA.
AC   W1NJA2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN   ORFNames=AMTR_s00060p00116070 {ECO:0000313|EMBL:ERM95857.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM95857.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
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         Evidence={ECO:0000256|RuleBase:RU004356};
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC       ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; KI397373; ERM95857.1; -; Genomic_DNA.
DR   RefSeq; XP_006828441.1; XM_006828378.2.
DR   AlphaFoldDB; W1NJA2; -.
DR   STRING; 13333.W1NJA2; -.
DR   EnsemblPlants; ERM95857; ERM95857; AMTR_s00060p00116070.
DR   GeneID; 18423781; -.
DR   Gramene; ERM95857; ERM95857; AMTR_s00060p00116070.
DR   KEGG; atr:18423781; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_0_1_1; -.
DR   OMA; VLCEAMK; -.
DR   OrthoDB; 1115057at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IBA:GO_Central.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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:SF118; GLUTAMINE SYNTHETASE; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004356};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU004356};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          106..356
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   356 AA;  39281 MW;  BD430AED5016EDCE CRC64;
     MSILTDLLNL DLTDCTTKII AEYIWVGGSG MDLRSKARTI SSPVNSPKQL PKWNYDGSST
     GQAAGHDSEV ILYPQAIFPD PFRRGKNILV ICDTYAPDGT PIATNKRAAA EKIFSNPQVV
     AEEPWYGLEQ EYTLLQKDVK WPLGWPIGGF PGPQGPYYCG IGADKAWGRD VVDSHYKACL
     YAGINISGIN GEVMPGQWEF QVGPSEGISA GDELWCARYI LERITEIAGV VLTFDPKPIQ
     GDWNGAGCHT NYSTKSTRKE GGYEVIKKAI EKLGLRHKEH IAAYGEGNER RLTGHHETAD
     INTFSWGVAN RGASVRVGRD TEKEGRGYFE DRRPASNMDP YVVTSMIAET TILWNS
//
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