ID   GLNA2_CHLRE             Reviewed;         380 AA.
AC   Q42689;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Glutamine synthetase, chloroplastic;
DE            EC=6.3.1.2;
DE   AltName: Full=GS2;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   Flags: Precursor;
GN   Name=GLN2;
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: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; U46208; AAB01818.1; -; mRNA.
DR   PIR; T08090; T08090.
DR   AlphaFoldDB; Q42689; -.
DR   SMR; Q42689; -.
DR   STRING; 3055.EDP03611; -.
DR   ProMEX; Q42689; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   GO; GO:0009507; C:chloroplast; 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; Chloroplast; Ligase; Nucleotide-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..380
FT                   /note="Glutamine synthetase, chloroplastic"
FT                   /id="PRO_0000011176"
FT   DOMAIN          35..125
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          132..380
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   380 AA;  41285 MW;  7BD53794374E6A8C CRC64;
     MAFALRGVTA KASGRTAGAR SSGRTLTVRV QAYGMAAEYI WADGNEGKPE KGMIFNEMRS
     KTKCFEAPLG LDASEYPDWS FDGSSTGQAE GNNSDCILRP VRVVTDPIRG APHVLVMCEV
     FAPDGKPHST NTRAKLREII DDKVTAEDCW YGFEQEYTML AKTSGHIYGW PAGGFPAPQG
     PFYCGVGAES AFGRPLAEAH MEACMKAGLV ISGINAEVMP GQWEYQIGPV GPLALGDEVM
     LSRWLLHRLG EDFGIVSTFN PKPVRTGDWN GTGAHTNFST KGMRVPGGMK VIEEAVEKLS
     KTHIEHITQY GIGNEARLTG KHETCDINTF KHGVADRGSS IRIPLPVMLK GYGYLEDRRP
     AANVDPYTVA RLLIKTVLKG