ID   GLNA1_MAIZE             Reviewed;         357 AA.
AC   P38559;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Glutamine synthetase root isozyme 1;
DE            EC=6.3.1.2;
DE   AltName: Full=GS122;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN6; Synonyms=GS1-1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. A188; TISSUE=Seedling;
RX   PubMed=8106013; DOI=10.1007/bf00029015;
RA   Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., Snustad D.P.;
RT   "Differential expression of six glutamine synthetase genes in Zea mays.";
RL   Plant Mol. Biol. 23:401-407(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf;
RA   Sakakibara H., Kawabata S., Takahashi H., Hase T., Sugiyama T.;
RT   "Molecular cloning of the family of glutamine synthetase genes from maize:
RT   expression of genes for glutamine synthetase and ferredoxin-dependent
RT   glutamate synthase in photosynthetic and non-photosynthetic tissues.";
RL   Plant Cell Physiol. 33:49-58(1992).
RN   [3]
RP   SEQUENCE REVISION.
RA   Sakakibara H.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the flow of nitrogen into nitrogenous organic
CC       compounds.
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: Found mainly in the cortical tissues of seedling
CC       roots, and in the root tip.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X65926; CAA46719.1; -; mRNA.
DR   EMBL; D14579; BAA03433.1; -; mRNA.
DR   PIR; S39477; S39477.
DR   RefSeq; NP_001105538.1; NM_001112068.2.
DR   AlphaFoldDB; P38559; -.
DR   SMR; P38559; -.
DR   STRING; 4577.GRMZM2G050514_P03; -.
DR   PaxDb; P38559; -.
DR   PRIDE; P38559; -.
DR   GeneID; 542520; -.
DR   KEGG; zma:542520; -.
DR   MaizeGDB; 17151; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   OrthoDB; 784869at2759; -.
DR   SABIO-RK; P38559; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P38559; baseline and differential.
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: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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Glutamine synthetase root isozyme 1"
FT                   /id="PRO_0000153178"
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"
FT   CONFLICT        48
FT                   /note="I -> S (in Ref. 2; BAA03433)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  39250 MW;  912A5E3BAF9CC2B8 CRC64;
     MASLTDLVNL DLSDCTDRII AEYIWIGGTG IDLRSKARTV KGPITDPIQL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFKD PFRKGNHILV MCDCYTPQGE PIPTNKRYSA AKVFSHPDVA
     AEVPWYGIEQ EYTLLQKDVS WPLGWPVGGY PGPQGPYYCA AGADKAFGRD VVDAHYKACL
     YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWVARYI LERITEMAGI VLSLDPKPIK
     GDWNGAGAHT NYSTKSMREA GGYEVIKAAI DKLGKRHKEH IAAYGEGNER RLTGRHETAD
     INTFKWGVAN RGASIRVGRD TEREGKGYFE DRRPASNMDP YVVTGMIAET TILWNGN