ID   GLNA2_DAUCA             Reviewed;         432 AA.
AC   O22506;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, 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   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. US-Harumakigosun; TISSUE=Leaf;
RA   Higashi K., Kamada H.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The light-modulated chloroplast enzyme, encoded by a nuclear
CC       gene and expressed primarily in leaves, is responsible for the
CC       reassimilation of the ammonia generated by photorespiration.
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; AF019561; AAB71693.1; -; mRNA.
DR   PIR; T14292; T14292.
DR   AlphaFoldDB; O22506; -.
DR   SMR; O22506; -.
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           ?..432
FT                   /note="Glutamine synthetase, chloroplastic"
FT                   /id="PRO_0000011177"
FT   DOMAIN          79..159
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          166..432
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   432 AA;  47764 MW;  20EC0A4CF8E35345 CRC64;
     MAQILAPSVQ WQMRFTKNST EVSSMTSKMW GSLFLKQNKK APARSSTKYR ALAVKSEDGT
     INRMEDLLNL DVTPYTDKII AEYIWIGGTG IDVRSKSRTI SKPVEHPSEL PKWNYDGSST
     GQAPGDDSEV ILYPQAIFKD PFRGGNNILV ICDTYTPQGE PIPTNKRHKA AQIFSDAKVL
     GEVPWFGIEQ EYTLMQQDVN WPLGWNVGGY PGPQGPYYCA AGADKSFGRD ISDAHYKACL
     YAGINISGTN GEVMPGQWEF QVGPSVGIEA GDHIWCARYL LERITEQAGV VLTLDPKPID
     GDWNGAGCHT NYSTKSMREE GGFEVIKKAI LNLSLRHKEH ISAYGEGNER RLTGKHETAS
     IDSFSWGVAD RGCSIRVGRD TEKEGKGYLE DRRPASNMDP YVVTGLLAET TLLWEPTLEA
     EALAAQKLSL NV