ID   GLNA4_PHAVU             Reviewed;         429 AA.
AC   P15102;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Glutamine synthetase leaf isozyme, chloroplastic;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   AltName: Full=Isozyme delta;
DE   Flags: Precursor;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Tendergreen; TISSUE=Leaf;
RX   AGRICOLA=IND92000070; DOI=10.1007/BF00015671;
RA   Lightfoot D.A., Green N.K., Cullimore J.V.;
RT   "The chloroplast-located glutamine synthetase of Phaseolus vulgaris L.:
RT   nucleotide sequence, expression in different organs and uptake into
RT   isolated chloroplasts.";
RL   Plant Mol. Biol. 11:191-202(1988).
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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and stems. Low levels detected
CC       in roots and nodules. {ECO:0000269|Ref.1}.
CC   -!- MISCELLANEOUS: There are at least four isozymes of this enzyme in
CC       P.vulgaris.
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; X12738; CAA31234.1; -; mRNA.
DR   PIR; S04031; AJFBQD.
DR   RefSeq; XP_007147796.1; XM_007147734.1.
DR   RefSeq; XP_007147797.1; XM_007147735.1.
DR   AlphaFoldDB; P15102; -.
DR   SMR; P15102; -.
DR   STRING; 3885.XP_007147796.1; -.
DR   PRIDE; P15102; -.
DR   ProMEX; P15102; -.
DR   EnsemblPlants; ESW19790; ESW19790; PHAVU_006G155800g.
DR   EnsemblPlants; ESW19791; ESW19791; PHAVU_006G155800g.
DR   GeneID; 18628920; -.
DR   Gramene; ESW19790; ESW19790; PHAVU_006G155800g.
DR   Gramene; ESW19791; ESW19791; PHAVU_006G155800g.
DR   KEGG; pvu:PHAVU_006G155800g; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   OMA; DRRPNAN; -.
DR   OrthoDB; 784869at2759; -.
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; Nitrogen fixation; Nucleotide-binding;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           51..429
FT                   /note="Glutamine synthetase leaf isozyme, chloroplastic"
FT                   /id="PRO_0000011183"
FT   DOMAIN          76..156
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          160..429
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   429 AA;  47246 MW;  0CA55624B1118AF8 CRC64;
     MAQILAPSTQ WQMRFTKSSR HASPITSNTW SSLLMKQNKK TSSAKFRVLA VKSDGSTINR
     LEGLLNLDIT PFTDKIIAEY IWIGGTGIDV RSKSRTISKP VEHPSELPKW NYDGSSTGQA
     PGEDSEVILY PQAIFKDPFR GGNNILVICD AYTPAGEPIP TNKRHRAAEV FSNPRVIAEV
     PWFGIEQEYT LLQTNVNWPL GWPVGGYPGP QGPYYCSAGA DKSFGRDISD AHYKACLFAG
     INISGTNGEV MPGQWEYQVG PSVGIEAGDH IWASRYILER ITEQAGVVLS LDPKPIEGDW
     NGAGCHTNYS TKSMREDGGF EVIKKAILNL SLRHKEHISA YGEGNERRLT GKHETASINT
     FSWGVANRGC SIRVGRDTEK NGKGYLEDRR PASNMDPYVV TSLLAESTLL WEPTLEAEAL
     AAQKLALKV