ID GLN1B_PROHU Reviewed; 469 AA. AC P28786; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 08-NOV-2023, entry version 100. 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 Proteus hauseri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=183417; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / RC NCTC 4175 / NRRL B-3405; RX PubMed=8095910; DOI=10.1111/j.1574-6968.1993.tb05952.x; RA Steglitz-Moersdorf U., Moersdorf G., Kaltwasser H.; RT "Cloning, heterologous expression, and sequencing of the Proteus vulgaris RT glnAntrBC operon and implications of nitrogen control on heterologous RT urease expression."; RL FEMS Microbiol. Lett. 106:157-164(1993). 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; X68129; CAA48234.1; -; Genomic_DNA. DR PIR; S23899; S23899. DR RefSeq; WP_064718176.1; NZ_PGWU01000008.1. DR AlphaFoldDB; P28786; -. DR SMR; P28786; -. DR STRING; 1354271.M997_0110; -. DR OrthoDB; 9807095at2; -. 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..469 FT /note="Glutamine synthetase" FT /id="PRO_0000153250" FT DOMAIN 13..97 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 105..469 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 130 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WN39" 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 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; 52205 MW; 852EE660D070E61A CRC64; MSLEHVLSMI EEHKVRYIDL RFTDTRGKEQ HLTIPAHQVN DDFFEEGKMF DGSSIGGWKG INESDMVLMP DASTAMLDPF FQDPTLIIRC DVLEPGTMQG YDRDPRSISK RAEDYLKSSG IADTVLFGPE PEFFLFDDIR FKNDISGASY AINDIEAAWN TNTKYEDGNK GHRPMVKGGY FPLPPVDSSQ DIRSTMCNIM EEMGLVVEAH HHEVATAGQN EVATRFNTMT KKADETQIYK YVVQNVAHVF GKTATFMPKP LVGDNGSGMH CHMSLSKNGT NLFAGDKYGG LSEMALYYIG GIIKHARALN AFTNPTTNSY KRLVPGFEAP VMLAYSARNR SASIRIPVVA SMKARRIEVR FPDPLANPYL AFAAQLMAGL DGITNKIHPG DAMDKNLYDL PPEEAKEIPT VAGSLEEALN ALDADREFLT HGGVFTNDSI DAYLALLRTD VQRVRMAPHP LEFEMYYSA //