ID   GLNA2_MAIZE             Reviewed;         368 AA.
AC   P38560;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Glutamine synthetase root isozyme 2;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN2; Synonyms=GS1-2;
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).
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 vascular tissues of seedling
CC       roots.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {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; X65927; CAA46720.1; -; mRNA.
DR   PIR; S39478; S39478.
DR   AlphaFoldDB; P38560; -.
DR   SMR; P38560; -.
DR   STRING; 4577.P38560; -.
DR   PaxDb; 4577-GRMZM2G024104_P01; -.
DR   MaizeGDB; 17151; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   InParanoid; P38560; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P38560; 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:SF92; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-3; 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..368
FT                   /note="Glutamine synthetase root isozyme 2"
FT                   /id="PRO_0000153179"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..368
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   REGION          38..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  40094 MW;  32F1E1AE109AEA0D CRC64;
     MALLSDLINL DLSGRTGKII AEYIWVGGSG MDVRSKARTL SGPVDDPSKL PKWNFDGSST
     GQAPGDDSEV ILCPRAIFRD PFRKGQNILV MCDCYEPNGE PIPSNKRHGA AKIFSHPDVK
     AEEPWFGIEQ EYTLLQKDTK WPLGWPLAYP GPQGPYYCAA GADKSYGRDI VDCAYKACLY
     AGIDISGING EVMPGQWEFQ VAPAVGVSAG DQLWVARYIL ERITEIAGVV VSFDPKPIPG
     DWNGAGAHTN YSTKSMRSDG GYEVIKKAIG KLGLRHREHI AAYGDGNERP LTGRHETADI
     NTFVWGVPNR GASVRVGRDT EKEGKGYFED RRPASNMDPY VVTCLIAETT MLWEPSHSNG
     DGKGAAAP
//