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 27-MAR-2024, entry version 128. 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}. 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; 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.P38561; -. DR PaxDb; 4577-GRMZM5G872068_P01; -. DR GeneID; 542214; -. DR KEGG; zma:542214; -. DR MaizeGDB; 17151; -. DR eggNOG; KOG0683; Eukaryota. DR InParanoid; P38561; -. DR OrthoDB; 1115057at2759; -. 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: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 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 //