ID   GLNA1_CHLRE             Reviewed;         382 AA.
AC   Q42688;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 111.
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   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=A55;
RX   PubMed=8938407; DOI=10.1104/pp.112.3.987;
RA   Chen Q., Silflow C.D.;
RT   "Isolation and characterization of glutamine synthetase genes in
RT   Chlamydomonas reinhardtii.";
RL   Plant Physiol. 112:987-996(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   -!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
CC       phosphinothricin (PPT).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U46207; AAB01817.1; -; mRNA.
DR   PIR; T08088; T08088.
DR   RefSeq; XP_001699902.1; XM_001699850.1.
DR   AlphaFoldDB; Q42688; -.
DR   SMR; Q42688; -.
DR   STRING; 3055.EDP07598; -.
DR   ProMEX; Q42688; -.
DR   EnsemblPlants; PNW87204; PNW87204; CHLRE_02g113200v5.
DR   GeneID; 5725229; -.
DR   Gramene; PNW87204; PNW87204; CHLRE_02g113200v5.
DR   KEGG; cre:CHLRE_02g113200v5; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_1_1_1; -.
DR   OrthoDB; 784869at2759; -.
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..382
FT                   /note="Glutamine synthetase cytosolic isozyme"
FT                   /id="PRO_0000153169"
FT   DOMAIN          36..118
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          135..382
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   382 AA;  42146 MW;  CC806E221EE461F5 CRC64;
     MAAGSVGVFA TDEKIGSLLD QSITRHFLST VTDQQGKICA EYVWIGGSMH DVRSKSRTLS
     TIPTKPEDLP HWNYDGSSTG QAPGHDSEVY LIPRSIFKDP FRGGDNILVM CDCYEPPKVN
     PDGTLAAPKP IPTNTRFACA EVMEKAKKEE PWFGIEQEYT LLNAITKWPL GWPKGGYPAP
     QGPYYCSAGA GVAIGRDVAE VHYRLCLAAG VNISGVNAEV LPSQWEYQVG PCEGITMGDH
     MWMSRYIMYR VCEMFNVEVS FDPKPIPGDW NGSGGHTNYS TKATRTAPDG WKVIQEHCAK
     LEARHAVHIA AYGEGNERRL TGKHETSSMS DFSWGVANRG CSIRVGRMVP VEKSGYYEDR
     RPASNLDAYV VTRLIVETTI LL