ID   GLNA1_PEA               Reviewed;         355 AA.
AC   P08282;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Glutamine synthetase nodule isozyme;
DE            EC=6.3.1.2;
DE   AltName: Full=Cytosolic GS1;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GS1;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2898472; DOI=10.1016/s0021-9258(19)81566-1;
RA   Tingey S.V., Tsai F., Edwards J., Walker E.L., Coruzzi G.M.;
RT   "Chloroplast and cytosolic glutamine synthetase are encoded by homologous
RT   nuclear genes which are differentially expressed in vivo.";
RL   J. Biol. Chem. 263:9651-9657(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 97-355.
RC   STRAIN=cv. Sparkle;
RX   PubMed=2884100; DOI=10.1002/j.1460-2075.1987.tb04710.x;
RA   Tingey S.V., Walker E.L., Coruzzi G.M.;
RT   "Glutamine synthetase genes of pea encode distinct polypeptides which are
RT   differentially expressed in leaves, roots and nodules.";
RL   EMBO J. 6:1-9(1987).
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   -!- MISCELLANEOUS: In pea there are distinct isozymes in leaves, roots and
CC       nodules.
CC   -!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
CC       phosphinothricin (PPT).
CC   -!- MISCELLANEOUS: This root isozyme is responsible for the assimilation of
CC       ammonia fixed by bacteroids.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; M20663; AAA33669.1; -; mRNA.
DR   EMBL; X05515; CAA29058.1; -; mRNA.
DR   PIR; B28089; AJPMQ1.
DR   AlphaFoldDB; P08282; -.
DR   SMR; P08282; -.
DR   PRIDE; P08282; -.
DR   GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding.
FT   CHAIN           1..355
FT                   /note="Glutamine synthetase nodule isozyme"
FT                   /id="PRO_0000153188"
FT   DOMAIN          18..98
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          105..355
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   355 AA;  38928 MW;  2AB833FAD7AA3687 CRC64;
     MSLSDLINLD LSGTTEKIIA EYIWIGGSGL DLRCKARTLP GPVTDPSELP KWNYDGSSTG
     QAPGQDSEVI LYPQAIFKDP FRRGNHILVM CDAYSPAGEP IPTNKRHAAA KVFSHPDVVA
     EETWYGIEQE YTLLQKDINW PLGWPAGGYP GPQGPYYCSV GADKAFGRDV VEAHYKACLF
     AGINISGING EVMPGQWEFQ VGPSVGISAG DEIWVARYIL ERITEVAGVV LTFDPKPIKG
     DWNGAGAHTN YSTKSMREDG GYEIIKKAIE KLGKRLPEHI SAYGEGNERR LTGKHETADI
     NTFSWGVANR GASVRVGRDT EKEGKGYFED RRPASNMDPY VVTSMIAETT ILLKP