ID   GLNA1_ALNGL             Reviewed;         356 AA.
AC   O04867;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=GS(1);
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN1;
OS   Alnus glutinosa (European alder) (Betula alnus var. glutinosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Alnus.
OX   NCBI_TaxID=3517;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RX   PubMed=9002618; DOI=10.1007/bf00041403;
RA   Guan C., Ribeiro A., Akkermans A.D.L., Jing Y., van Kammen A.,
RA   Bisseling T., Pawlowski K.;
RT   "Nitrogen metabolism in actinorhizal nodules of Alnus glutinosa: expression
RT   of glutamine synthetase and acetylornithine transaminase.";
RL   Plant Mol. Biol. 32:1177-1184(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   -!- TISSUE SPECIFICITY: Found at highest levels in root nodules.
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; Y08681; CAA69937.1; -; mRNA.
DR   AlphaFoldDB; O04867; -.
DR   SMR; O04867; -.
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"
FT                   /id="PRO_0000153167"
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;  39324 MW;  5A768FF0C13B5A33 CRC64;
     MSLLSDLINL NLSDATDKVI AEYIWIGGSG TDLRSKARTL TGPVNHPSKL PKWNYDGSST
     GQAPGEDSEV IYILRQFFKD PFRRGNNILV ICDTYTPAGE PIPTNKRHGA AKIFSHPEVV
     AEVPWYGIEQ EYTLLQKDVK WPLGWPVGGY PGPQGPYYCG IGADKAWGRD IVDAHYKACL
     YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEVWAARYI LERITEIAGV VLSLDPKPIQ
     GDWNGAGAHT NYSTKSMRNN GGYEIIKKAI EKLGLRHKEH IAAYGEGNER RLTGRHETAD
     INTFKWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TLLWKP