ID   GLNA1_LOTJA             Reviewed;         356 AA.
AC   Q42899; O04880;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme;
DE            EC=6.3.1.2;
DE   AltName: Full=GS1;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN1;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Root;
RA   Ruiz M.T., Prosser I.M., Clarkson D.T.;
RT   "Cloning of a subunit of the cytosolic glutamine synthetase from Lotus
RT   japonicus.";
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9323367; DOI=10.1007/s004380050537;
RA   Thykjaer T., Danielsen D., She Q., Stougaard J.;
RT   "Organization and expression of genes in the genomic region surrounding the
RT   glutamine synthetase gene Gln1 from Lotus japonicus.";
RL   Mol. Gen. Genet. 255:628-636(1997).
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   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X94299; CAA63963.1; -; mRNA.
DR   EMBL; Y12859; CAA73366.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q42899; -.
DR   SMR; Q42899; -.
DR   PRIDE; Q42899; -.
DR   ProMEX; Q42899; -.
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 cytosolic isozyme"
FT                   /id="PRO_0000153175"
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          37..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        35
FT                   /note="S -> T (in Ref. 2; CAA73366)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="N -> Y (in Ref. 1; CAA63963)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  39147 MW;  F31F8696F645F731 CRC64;
     MSLLSDLINL NLSETTDKII AEYIWIGGSG LDMRSKARTL PGPVSDPSQL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFRD PFRRGSNILV ICDAYTPAGE PIPTNKRHAA AKVFSHPDVV
     AEVPWYGIEQ EYTLLQKEVN WPVGWPIGGF PGPQGPYYCG IGADKAFGRD IVDAHYKACL
     YAGVNISGIN GEVMPGQWEF QVGPSVGISA GDEVWVARYI LERITEIAGV VLSFDPKPIK
     GDWNGAGAHT NYSTKTMRED GGYEVIKKAI DKLGLRHKEH IAAYGEGNER RLTGRHETAD
     INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIADT TILWKP