ID GLN1B_ACIFR Reviewed; 468 AA. AC P07804; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 24-JAN-2024, entry version 108. 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 Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans). OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=920; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2886400; DOI=10.1016/0378-1119(87)90009-6; RA Rawlings D.E., Jones W.A., O'Neill E.G., Woods D.R.; RT "Nucleotide sequence of the glutamine synthetase gene and its controlling RT region from the acidophilic autotroph Thiobacillus ferrooxidans."; RL Gene 53:211-217(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; M16626; AAA27370.1; -; Genomic_DNA. DR PIR; A29460; AJBCQF. DR AlphaFoldDB; P07804; -. DR SMR; P07804; -. 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 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 InterPro; IPR027302; Gln_synth_N_conserv_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; PS00180; GLNA_1; 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 Nucleotide-binding; Phosphoprotein. FT CHAIN 1..468 FT /note="Glutamine synthetase" FT /id="PRO_0000153274" FT DOMAIN 15..100 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 107..468 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 132 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 213 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 264..265 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 265 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 269 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 271..273 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 273 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 321 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 327 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 339 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 339 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 344 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 352 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 357 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 359 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT MOD_RES 397 FT /note="O-AMP-tyrosine" FT /evidence="ECO:0000250|UniProtKB:P9WN39" SQ SEQUENCE 468 AA; 51614 MW; 24710B272B3A7054 CRC64; MGYSPSDVVK LIQEKDIKFI DFRFTDTKGK EQHVSVPGHV IEEDTFTEGK AFDGSSIAGW KGINESDMIL LPDPDSAVLD PFMDETTLLL RCDVIEPATG QGYERDPRSV AKRAEIYLKS TGIADTSFFG PEFFVFDSVT WNIDMSGCAY KVDAEEAAWN SGKEYESGNM GHRLGVKGGY FPVPPVDSAQ DLRSAMCLAM EEMGLKVEVH HHEVATAGQH EIGVGFNTLT PRRMRCKILK YVVHNVAAVR QTATFMPKPV VGDNGSGMHV HQSLGKDGKN IFAGDLYGGL SEIALYYIGG IIKHAKAVNA LTNPSTNSYK RLVPHFEAPV LLAYSAKNRS ASIRIPYVNS PKARRIEVRF PDSTANPYLA FSAMLMAGLD GIQNKIHPAT AMDKNLYDLP AEEQANIPGV AASLEEALRA LEADHDFLMK GGVFSESWLE GYLDVKWAEV QTLRVTTHPV EFQMYYSL //