ID   GLNA3_PEA               Reviewed;         357 AA.
AC   P07694; Q43065;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Glutamine synthetase root isozyme A;
DE            EC=6.3.1.2;
DE   AltName: Full=Cytosolic GS3 A;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GS3A;
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].
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Feltham First;
RX   PubMed=8616212; DOI=10.1007/bf00020456;
RA   Walker E.L., Weeden N.F., Taylor C.B., Green P., Coruzzi G.M.;
RT   "Molecular evolution of duplicate copies of genes encoding cytosolic
RT   glutamine synthetase in Pisum sativum.";
RL   Plant Mol. Biol. 29:1111-1125(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC   STRAIN=cv. Sparkle;
RX   PubMed=1688248; DOI=10.1111/j.1365-313x.1991.00235.x;
RA   Brears T., Walker E.L., Coruzzi G.M.;
RT   "A promoter sequence involved in cell-specific expression of the pea
RT   glutamine synthetase GS3A gene in organs of transgenic tobacco and
RT   alfalfa.";
RL   Plant J. 1:235-244(1991).
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   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB03492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X04763; CAA28456.1; -; mRNA.
DR   EMBL; U28924; AAB03492.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X60832; CAA43223.1; -; Genomic_DNA.
DR   PIR; B26171; AJPMQA.
DR   PIR; S62711; S62711.
DR   AlphaFoldDB; P07694; -.
DR   SMR; P07694; -.
DR   PRIDE; P07694; -.
DR   EnsemblPlants; Psat0s690g0040.1; Psat0s690g0040.1.cds; Psat0s690g0040.
DR   EnsemblPlants; Psat0s690g0040.2; Psat0s690g0040.2.cds; Psat0s690g0040.
DR   Gramene; Psat0s690g0040.1; Psat0s690g0040.1.cds; Psat0s690g0040.
DR   Gramene; Psat0s690g0040.2; Psat0s690g0040.2.cds; Psat0s690g0040.
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..357
FT                   /note="Glutamine synthetase root isozyme A"
FT                   /id="PRO_0000153189"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..357
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   357 AA;  39288 MW;  F50C83DBB6FADDEB CRC64;
     MSSLSDLINF NLSDSTEKII AEYIWVGGSG IDIRSKARTL PGPVSDPAKL PKWNYDGSST
     NQAPGKDSEV ILYPQAIFKD PFRRGNNILV ICDVYTPAGE PLPTNKRYNA AKIFSHPDVA
     AEVPWYGIEQ EYTLLQKDIN WPLGWPIGGY PGKQGPYYCG IGADKAYGRD IVDAHYKACL
     FAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWAARYI LERITEIAGV VVSFDPKPIP
     GDWNGAGAHA NFSTKSMREN GGYEVIKKAI EKLGLRHKEH IAAYGEGNER RLTGKHETAD
     INVFSWGVAN RGSSIRVGRD TEKDGKGYFE DRRPASNMDP YVVTSMIAET TILWKKP