ID   GLNA2_PHAVU             Reviewed;         356 AA.
AC   P04771;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Glutamine synthetase PR-2;
DE            EC=6.3.1.2;
DE   AltName: Full=Gln isozyme alpha;
DE   AltName: Full=Glutamate--ammonia ligase;
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].
RX   PubMed=16453687; DOI=10.1002/j.1460-2075.1986.tb04379.x;
RA   Gebhardt C., Oliver J.E., Forde B.G., Saarelainen R., Miflin B.J.;
RT   "Primary structure and differential expression of glutamine synthetase
RT   genes in nodules, roots and leaves of Phaseolus vulgaris.";
RL   EMBO J. 5:1429-1435(1986).
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: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Roots.
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; X04002; CAA27632.1; -; mRNA.
DR   PIR; B26308; AJFBQA.
DR   RefSeq; XP_007152660.1; XM_007152598.1.
DR   AlphaFoldDB; P04771; -.
DR   SMR; P04771; -.
DR   EnsemblPlants; ESW24654; ESW24654; PHAVU_004G148300g.
DR   GeneID; 18633095; -.
DR   Gramene; ESW24654; ESW24654; PHAVU_004G148300g.
DR   KEGG; pvu:PHAVU_004G148300g; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   OMA; CAIGANK; -.
DR   OrthoDB; 1115057at2759; -.
DR   PhylomeDB; P04771; -.
DR   BRENDA; 6.3.1.2; 4746.
DR   SABIO-RK; P04771; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR008147; Gln_synt_N.
DR   InterPro; IPR036651; Gln_synt_N_sf.
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   PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF110; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-2; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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; Nitrogen fixation; Nucleotide-binding.
FT   CHAIN           1..356
FT                   /note="Glutamine synthetase PR-2"
FT                   /id="PRO_0000153192"
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..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  39205 MW;  0001776952B2E0EC CRC64;
     MSLLSDLINL NLSESTEKII AEYIWVGGSG MDLRSKARTL PGPVDDPAKL PKWNYDGSST
     DQAPGDDSEV ILYPQAIFKD PFRRGNNILV ICDVYTPAGE PLPTNKRYDA AKIFSHPDVV
     AEVPWYGIEQ EYTLLQKDVN WPLGWPLGGY PGPQGPYYCG VGADKAYGRD IVDAHYKACV
     YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEVWAARYI LERITELAGA VVSFDPKPIP
     GDWNGAGAHS NYSTKSMREE GGYEVIKKAI EKLGLRHKEH IAAYGKGNER RLTGRHETAD
     INTFSWGVAN RGSSVRVGRD TEKQGKGYFE DRRPASNMDP YVVTSMIAET TILWKP
//