ID   GLNA5_MAIZE             Reviewed;         357 AA.
AC   P38563;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Glutamine synthetase root isozyme 5;
DE            EC=6.3.1.2;
DE   AltName: Full=GS117;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GS1-5;
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. 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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-357.
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).
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, stem and seedling shoot.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; D14578; BAA03432.1; ALT_SEQ; mRNA.
DR   EMBL; X65930; CAA46723.1; -; mRNA.
DR   PIR; S39481; S39481.
DR   AlphaFoldDB; P38563; -.
DR   SMR; P38563; -.
DR   STRING; 4577.P38563; -.
DR   MaizeGDB; 17151; -.
DR   InParanoid; P38563; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P38563; 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:glutamine synthetase activity; IBA:GO_Central.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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:SF109; 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; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Glutamine synthetase root isozyme 5"
FT                   /id="PRO_0000153182"
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        139
FT                   /note="L -> V (in Ref. 2; CAA46723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="R -> K (in Ref. 2; CAA46723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285..286
FT                   /note="GE -> DG (in Ref. 2; CAA46723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        313
FT                   /note="A -> G (in Ref. 2; CAA46723)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  39259 MW;  183F9C15F2FF33A6 CRC64;
     MASLTDLVNL DLSDCTDKII AEYIWVGGSG IDLRSKARTV KGPITDPSQL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFKD PFRKGNNILV MCDCYTPQGE PIPSNKRYKA ATVFSHPDVA
     AEVPWYGIEQ EYTLLQKDLS WPLGWPVGGY PGPQGPYYCA AGADKAFGRD VVDAHYKACL
     YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWVARYI LERITEMAGI VLSLDPKPIK
     GDWNGAGAHT NYSTKSMREA GGYEVIKEAI EKLGRRHREH IAAYGEGNER RLTGRHETAD
     INTFKWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTGMIADT TILWKGN
//