ID   GLNA4_MAIZE             Reviewed;         355 AA.
AC   P38562;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Glutamine synthetase root isozyme 4;
DE            EC=6.3.1.2;
DE   AltName: Full=GS107;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN5; Synonyms=GS1-4;
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).
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 in all the tissues examined with higher
CC       expression found in tissues of the root, stem and seedling shoot.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X65929; CAA46722.1; -; mRNA.
DR   EMBL; D14576; BAA03430.1; -; mRNA.
DR   PIR; S39480; S39480.
DR   AlphaFoldDB; P38562; -.
DR   SMR; P38562; -.
DR   STRING; 4577.P38562; -.
DR   MaizeGDB; 17151; -.
DR   InParanoid; P38562; -.
DR   BRENDA; 6.3.1.2; 6752.
DR   SABIO-RK; P38562; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P38562; 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:SF93; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-4; 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..355
FT                   /note="Glutamine synthetase root isozyme 4"
FT                   /id="PRO_0000153181"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..355
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   REGION          37..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        316
FT                   /note="A -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="Q -> RE (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   355 AA;  38981 MW;  02F891F1209C50E5 CRC64;
     MACLTDLVNL NLSDTTEKII AEYIWIGGSG MDLRSKARTL PGPVTDPSKL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDCYTPAGE PIPTNKRYSA AKIFSSPEVA
     AEEPWYGIEQ EYTLLQKDTN WPLGWPIGGF PGPQGPYYCG IGAEKSFGRD IVDAHYKACL
     YAGINISGIN GEVMPGQWEF QVGPSVGISS GDQVWVARYI LERITEIAGV VVTFDPKPIP
     GDWNGAGAHT NYSTESMRKE GGYEVIKAAI EKLKLRHKEH IAAYGEGNER RLTGRHETAD
     INTFSWGVAN RGASVAVGQT EQNGKGYFED RRPASNMDPY VVTSMIAETT IVWKP
//