ID GLNA2_RHILP Reviewed; 326 AA. AC Q02154; Q9R5J0; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 08-NOV-2023, entry version 94. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1357539}; DE Short=GS {ECO:0000303|PubMed:1357539}; DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P16580}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; DE AltName: Full=Glutamine synthetase II {ECO:0000303|PubMed:1357539}; DE Short=GSII {ECO:0000303|PubMed:1357539}; GN Name=glnII {ECO:0000303|PubMed:1357539}; OS Rhizobium leguminosarum bv. phaseoli. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=385; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RC STRAIN=LPR1105; RX PubMed=1357539; DOI=10.1007/bf00538692; RA Patriarca E.J., Chiurazzi M., Manco G., Riccio A., Lamberti A., Paolis A., RA Rossi M., Defez R., Iaccarino M.; RT "Activation of the Rhizobium leguminosarum glnII gene by NtrC is dependent RT on upstream DNA sequences."; RL Mol. Gen. Genet. 234:337-345(1992). RN [2] RP PROTEIN SEQUENCE OF 2-27, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT. RC STRAIN=LPR1105; RX PubMed=1355107; DOI=10.1099/00221287-138-7-1453; RA Manco G., Rossi M., Defez R., Lamberti A., Percuoco G., Iaccarino M.; RT "Dissociation by NH4Cl treatment of the enzymic activities of glutamine RT synthetase II from Rhizobium leguminosarum biovar viceae."; RL J. Gen. Microbiol. 138:1453-1460(1992). CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from CC glutamate and ammonia. {ECO:0000305|PubMed:1355107}. 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:P16580}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P16580}; CC -!- ACTIVITY REGULATION: Transferase activity is inhibited by NH(4)Cl. CC {ECO:0000269|PubMed:1355107}. CC -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000269|PubMed:1355107}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16580}. CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein NtrC. CC {ECO:0000269|PubMed:1357539}. CC -!- MISCELLANEOUS: Two forms of glutamine synthetase (GSI and GSII) can be CC found in this nitrogen fixing bacteria, GSI is a typical prokaryotic CC glutamine synthetase whereas GSII is similar to the eukaryotic enzyme. CC {ECO:0000305|PubMed:1357539}. 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; X67296; CAA47710.1; -; Genomic_DNA. DR PIR; S26216; S26216. DR AlphaFoldDB; Q02154; -. DR SMR; Q02154; -. 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; IPR027302; Gln_synth_N_conserv_site. DR PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 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 ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium; KW Metal-binding; Nitrogen fixation; Nucleotide-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1355107" FT CHAIN 2..326 FT /note="Glutamine synthetase" FT /id="PRO_0000153224" FT DOMAIN 4..85 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 83..326 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 107 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 109 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 164 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 169 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 275 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" SQ SEQUENCE 326 AA; 36979 MW; 637AE03B83D1F840 CRC64; MTKFKLEYIW LDGYTPVPNL RGKTQIKEFD EFPTLEQLPL WGFDGSSTMQ AEGSSDCVLK PVAIYPDPAR TNGALVMCEV MMPDGHAHAS NARATILDDE DAWFGFEQEY FFYQNGRPLG FPEQGYPAPQ PYYTGVGYSN VGDVAREIVE EHLDLCLAAG INHEGINAEV AKGQWEFQIF GKGSKKAADQ IWMARYLLQR LTEKYGIDIE YHCKPLGDTD WNGSGMHCNF STKYLREVGG KEYFEALMAS SDKNLMDHIA VYGPDNDKRL TGKHETAPWN KFSYGVADRG ASIRVPHSFI KNDYKGYLED RRPNSQGDPY QIVRRF //