ID GLN1B_RHILV Reviewed; 469 AA. AC P09826; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 08-NOV-2023, entry version 117. DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P0A1P6}; DE Short=GS {ECO:0000250|UniProtKB:P0A1P6}; DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P0A1P6}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; DE AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P0A1P6}; DE Short=GSI beta {ECO:0000250|UniProtKB:P0A1P6}; GN Name=glnA {ECO:0000250|UniProtKB:P0A1P6}; OS Rhizobium leguminosarum bv. viciae. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=387; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RCC1001; RX PubMed=2882467; DOI=10.1093/nar/15.5.1951; RA Colonna-Romano S., Riccio A., Guida M., Defez R., Lamberti A., RA Iaccarino M., Arnold W., Priefer U., Puehler A.; RT "Tight linkage of glnA and a putative regulatory gene in Rhizobium RT leguminosarum."; RL Nucleic Acids Res. 15:1951-1964(1987). CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from CC glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}. 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 Evidence={ECO:0000250|UniProtKB:P0A1P6}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P9WN39}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39}; CC -!- ACTIVITY REGULATION: The activity of this enzyme could be controlled by CC adenylation under conditions of abundant glutamine. CC {ECO:0000250|UniProtKB:Q3V5W6}. CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric CC ring. {ECO:0000250|UniProtKB:P0A1P6}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}. 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; X04880; CAA28569.1; -; Genomic_DNA. DR PIR; A26567; AJZRQL. DR AlphaFoldDB; P09826; -. DR SMR; P09826; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro. DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW. 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; IPR004809; Gln_synth_I. DR InterPro; IPR001637; Gln_synth_I_adenylation_site. DR NCBIfam; TIGR00653; GlnA; 1. DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR43407:SF2; GLUTAMINE SYNTHETASE; 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; PS00182; GLNA_ADENYLATION; 1. DR PROSITE; PS00181; GLNA_ATP; 1. DR PROSITE; PS51986; GS_BETA_GRASP; 1. DR PROSITE; PS51987; GS_CATALYTIC; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding; KW Nitrogen fixation; Nucleotide-binding; Phosphoprotein. FT CHAIN 1..469 FT /note="Glutamine synthetase" FT /id="PRO_0000153223" FT DOMAIN 14..99 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 106..469 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 131 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 133 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 214 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 265..266 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 266 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 272..274 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 274 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 322 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 328 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 340 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 340 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 345 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 358 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 360 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT MOD_RES 398 FT /note="O-AMP-tyrosine" FT /evidence="ECO:0000250|UniProtKB:P9WN39" SQ SEQUENCE 469 AA; 52233 MW; A1E158ECD0970FBC CRC64; MATASEILKQ IKENDVKFVD LRFTDRRASL QHVTMDVVCV DEDMFADGVM FDGFSIGGWK AINESDMVLM PDTETVHMDP FFAQSTMVIV CDILDPVSGE AYNRDRRGTA KKAEAYLKAS GIGDTVFVGR EAEFFVFDDV KYKADPYNTG FKLDSTELPS NDDTDYETGN LGHRPRVKGG YFPVPPVDSA QDMRSEMLTV LSEMGVVVEK HHHEVAAAQH DTLVRNADEL GIKFKMQIYK YVVHQVANAY GKTATFMPKP IFGDNGSGMH VHQSIWKGGK PTFAGDEYAG LSESCLFYIG GIIKHAKAIN AFTNPSTNSY KRFVPGYEAP VLLAYSARNR SASCRIPFGS NPKAKRVEVR FPDPTANPYL AFAAMLMAGL DGIKNKIHPG KAMDKDLYDL PPKELKKIPT VCGSLRQALE SLDKDRKFLT AGGVFDDDQI DAFIELKMAE VMRFEMTPHP VEYDMYYSA //