GLNA3_MAIZE
ID GLNA3_MAIZE Reviewed; 356 AA.
AC P38561;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Glutamine synthetase root isozyme 3;
DE EC=6.3.1.2;
DE AltName: Full=GS112;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=GLN4; Synonyms=GS1-3;
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.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X65928; CAA46721.1; -; mRNA.
DR EMBL; D14577; BAA03431.1; -; mRNA.
DR PIR; S39479; S39479.
DR RefSeq; NP_001105296.1; NM_001111826.1.
DR PDB; 2D3A; X-ray; 2.63 A; A/B/C/D/E/F/G/H/I/J=1-356.
DR PDB; 2D3B; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J=1-356.
DR PDB; 2D3C; X-ray; 3.81 A; A/B/C/D/E/F/G/H/I/J=1-356.
DR PDBsum; 2D3A; -.
DR PDBsum; 2D3B; -.
DR PDBsum; 2D3C; -.
DR AlphaFoldDB; P38561; -.
DR SMR; P38561; -.
DR STRING; 4577.GRMZM5G872068_P01; -.
DR PaxDb; P38561; -.
DR GeneID; 542214; -.
DR KEGG; zma:542214; -.
DR MaizeGDB; 17151; -.
DR eggNOG; KOG0683; Eukaryota.
DR OrthoDB; 784869at2759; -.
DR BRENDA; 6.3.1.2; 6752.
DR EvolutionaryTrace; P38561; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P38561; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..356
FT /note="Glutamine synthetase root isozyme 3"
FT /id="PRO_0000153180"
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"
FT CONFLICT 15
FT /note="T -> N (in Ref. 2; BAA03431)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..290
FT /note="DG -> ER (in Ref. 2; BAA03431)"
FT /evidence="ECO:0000305"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2D3A"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:2D3A"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 125..136
FT /evidence="ECO:0007829|PDB:2D3A"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2D3A"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 208..228
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:2D3B"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:2D3A"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:2D3A"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2D3A"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:2D3A"
SQ SEQUENCE 356 AA; 39169 MW; 0112DD32D5FB474C CRC64;
MACLTDLVNL NLSDTTEKII AEYIWIGGSG MDLRSKARTL SGPVTDPSKL PKWNYDGSST
GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDCYTPAGE PIPTNKRYNA AKIFSSPEVA
AEEPWYGIEQ EYTLLQKDTN WPLGWPIGGF PGPQGPYYCG IGAEKSFGRD IVDAHYKACL
YAGINISGIN GEVMPGQWEF QVGPSVGISS GDQVWVARYI LERITEIAGV VVTFDPKPIP
GDWNGAGAHT NYSTESMRKE GGYEVIKAAI EKLKLRHREH IAAYGEGNDG RLTGRHETAD
INTFSWGVAN RGASVRVGRE TEQNGKGYFE DRRPASNMDP YVVTSMIAET TIIWKP
