ID   GLNA2_SOYBN             Reviewed;         356 AA.
AC   O82560;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme 2;
DE            EC=6.3.1.2;
DE   AltName: Full=GS1-2;
DE   AltName: Full=Glutamate--ammonia ligase;
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Resnik; TISSUE=Root nodule;
RA   Morey K.J., Sengupta-Gopalan C.;
RT   "Soybean gene coding for a nodule specific glutamine synthetase.";
RL   (er) Plant Gene Register PGR98-194(1998).
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   -!- INTERACTION:
CC       O82560; O82560: -; NbExp=4; IntAct=EBI-10192111, EBI-10192111;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: This is a nodule isozyme.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; AF091456; AAC97935.1; -; Genomic_DNA.
DR   RefSeq; XP_003544980.1; XM_003544932.3.
DR   AlphaFoldDB; O82560; -.
DR   SMR; O82560; -.
DR   MINT; O82560; -.
DR   STRING; 3847.GLYMA14G39420.1; -.
DR   PRIDE; O82560; -.
DR   ProMEX; O82560; -.
DR   EnsemblPlants; KRH17323; KRH17323; GLYMA_14G213300.
DR   Gramene; KRH17323; KRH17323; GLYMA_14G213300.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_0_1_1; -.
DR   InParanoid; O82560; -.
DR   OrthoDB; 784869at2759; -.
DR   BRENDA; 6.3.1.2; 2483.
DR   Proteomes; UP000008827; Chromosome 14.
DR   Genevisible; O82560; GM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..356
FT                   /note="Glutamine synthetase cytosolic isozyme 2"
FT                   /id="PRO_0000153197"
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"
SQ   SEQUENCE   356 AA;  39208 MW;  4B9C63B7718656B5 CRC64;
     MSLLSDLINL NLSDITDKVI AEYIWVGGSG MDMRSKARTL SGPVKDPSKL PKWNYDGSST
     GQAPGQDSEV ILYPQAIFKD PFRRGSNILV MCDAYTPAGE PIPTNKRNNA AKIFGHPDVA
     AEEPWYGLEQ EYTLLQKDVQ WPLGWPLGGF PGPQGPYYCG TGANKAFGRD IVDSHYKACI
     YAGINISGIN GEVMPGQWEF QVGPSIGISA ADELWVARYI LERITEIAGV VLSFDPKPIQ
     GDWNGAGAHT NYSTKSMRND GGYEVIKKAI AKLEKRHKEH IAAYGEGNER RLTGRHETAD
     MNTFVWGVAN RGASIRVGRD TEKAGKGYFE DRRPASNMDP YVVTSMIAET TILWKP