ID   GLNA3_MEDSA             Reviewed;         356 AA.
AC   Q43785;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Glutamine synthetase nodule isozyme;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GS1;
OS   Medicago sativa (Alfalfa).
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; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Iroquois; TISSUE=Root nodule;
RX   PubMed=7756692; DOI=10.1094/mpmi-8-0218;
RA   Temple S.J., Heard J., Ganter G., Dunn K., Sengupta-Gopalan C.;
RT   "Characterization of a nodule-enhanced glutamine synthetase from alfalfa:
RT   nucleotide sequence, in situ localization, and transcript analysis.";
RL   Mol. Plant Microbe Interact. 8:218-227(1995).
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Iroquois; TISSUE=Root nodule;
RX   PubMed=2908768; DOI=10.1094/mpmi-1-066;
RA   Dunn K., Dickstein R., Feinbaum R., Burnett B.K., Peterman T.K.,
RA   Thoidis G., Goodman H.M., Ausubel F.M.;
RT   "Developmental regulation of nodule-specific genes in alfalfa root
RT   nodules.";
RL   Mol. Plant Microbe Interact. 1:66-74(1988).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Found at highest levels in root nodules.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; U15591; AAB41554.1; -; mRNA.
DR   AlphaFoldDB; Q43785; -.
DR   SMR; Q43785; -.
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 nodule isozyme"
FT                   /id="PRO_0000153184"
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;  39152 MW;  5368C4BD10C96ECB CRC64;
     MSLLSDLINL NLSESSEKII AEYIWVGGSG MDLRSKARTL PGPVSDPAKL PKWNYDGSST
     NQAPGQDSEV ILYPQAIFKD PFRQGNNILV ICDVYTPAGE PLPTNKRHNA AKIFSHPDVA
     AEVPWYGIEQ EYTLLQKDTN WPLGWPIGGF PGPQGPYYCG IGADKAYGRD IVDAHYKACL
     YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWAARYI LERITEIAGV VVSFDPKPIP
     GDWNGAGAHT NYSTKSMRED GGYEIIKKAI EKLGLRHKEH IAAYGEGNER RLTGKHETTD
     INTFSWGVAN RGASVRVGRD TEKDGKGYFE DRRPSSNMDP YVVTSMIAET TLLWKP
//