ID GLN1B_SALTY Reviewed; 469 AA. AC P0A1P6; P06201; Q60007; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 117. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2879772}; DE Short=GS {ECO:0000303|PubMed:2879772}; DE EC=6.3.1.2 {ECO:0000305|PubMed:7727369}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; DE AltName: Full=Glutamine synthetase I beta {ECO:0000305}; DE Short=GSI beta {ECO:0000305}; GN Name=glnA {ECO:0000303|PubMed:2879772}; OrderedLocusNames=STM4007; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2879772; DOI=10.1016/0378-1119(86)90415-4; RA Janson C.A., Kayne P.S., Almassy R.J., Grunstein M., Eisenberg D.; RT "Sequence of glutamine synthetase from Salmonella typhimurium and RT implications for the protein structure."; RL Gene 46:297-300(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-469. RC STRAIN=LT2; RA Kustu S.G.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH MANGANESE ION, RP COFACTOR, AND SUBUNIT. RX PubMed=2572586; DOI=10.2210/pdb2gls/pdb; RA Yamashita M.M., Almassy R.J., Janson C.A., Cascio D., Eisenberg D.; RT "Refined atomic model of glutamine synthetase at 3.5 A resolution."; RL J. Biol. Chem. 264:17681-17690(1989). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-469 IN COMPLEX WITH L-GLUTAMATE RP AND 2 MANGANESE IONS, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT. RX PubMed=8099447; DOI=10.1073/pnas.90.11.4996; RA Liaw S.H., Pan C., Eisenberg D.; RT "Feedback inhibition of fully unadenylylated glutamine synthetase from RT Salmonella typhimurium by glycine, alanine, and serine."; RL Proc. Natl. Acad. Sci. U.S.A. 90:4996-5000(1993). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 2-469 IN COMPLEX WITH AMP AND 2 RP MANGANESE IONS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT. RX PubMed=7727369; DOI=10.1021/bi00203a014; RA Liaw S.H., Jun G., Eisenberg D.; RT "Interactions of nucleotides with fully unadenylylated glutamine synthetase RT from Salmonella typhimurium."; RL Biochemistry 33:11184-11188(1994). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 2-469 IN COMPLEX WITH ADP; RP SUBSTRATE ANALOG AND 2 MANGANESE IONS, ACTIVITY REGULATION, COFACTOR, AND RP SUBUNIT. RX PubMed=11329256; DOI=10.1021/bi002438h; RA Gill H.S., Eisenberg D.; RT "The crystal structure of phosphinothricin in the active site of glutamine RT synthetase illuminates the mechanism of enzymatic inhibition."; RL Biochemistry 40:1903-1912(2001). CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from CC glutamate and ammonia. {ECO:0000269|PubMed:7727369}. 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:0000305|PubMed:7727369}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, CC ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447}; CC Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:11329256, CC ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, CC ECO:0000269|PubMed:8099447}; CC -!- ACTIVITY REGULATION: When cellular nitrogen levels are high, the C- CC terminal adenylyl transferase (AT) of GlnE inhibits GlnA by covalent CC transfer of an adenylyl group from ATP to Tyr-398. Conversely, when CC nitrogen levels are low, the N-terminal adenylyl removase (AR) of GlnE CC activates GlnA by removing the adenylyl group by phosphorolysis. The CC fully adenylated enzyme complex is inactive. CC {ECO:0000250|UniProtKB:Q3V5W6}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.58 mM for ATP {ECO:0000269|PubMed:7727369}; CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric CC ring. {ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, CC ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447}. 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; M14536; AAA27134.1; -; Genomic_DNA. DR EMBL; AE006468; AAL22846.1; -; Genomic_DNA. DR EMBL; X85104; CAA59423.1; -; Genomic_DNA. DR PIR; A25818; AJEBQT. DR RefSeq; NP_462887.1; NC_003197.2. DR RefSeq; WP_001271699.1; NC_003197.2. DR PDB; 1F1H; X-ray; 2.67 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469. DR PDB; 1F52; X-ray; 2.49 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469. DR PDB; 1FPY; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469. DR PDB; 1LGR; X-ray; 2.79 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469. DR PDB; 2GLS; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-469. DR PDB; 2LGS; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-469. DR PDBsum; 1F1H; -. DR PDBsum; 1F52; -. DR PDBsum; 1FPY; -. DR PDBsum; 1LGR; -. DR PDBsum; 2GLS; -. DR PDBsum; 2LGS; -. DR AlphaFoldDB; P0A1P6; -. DR SMR; P0A1P6; -. DR DIP; DIP-61253N; -. DR STRING; 99287.STM4007; -. DR BindingDB; P0A1P6; -. DR ChEMBL; CHEMBL5089; -. DR DrugBank; DB02663; 2-Amino-4-(Hydroxymethyl-Phosphinyl)Butanoic Acid. DR PaxDb; 99287-STM4007; -. DR GeneID; 1255533; -. DR KEGG; stm:STM4007; -. DR PATRIC; fig|99287.12.peg.4223; -. DR HOGENOM; CLU_017290_1_2_6; -. DR OMA; PHPHEFE; -. DR PhylomeDB; P0A1P6; -. DR BioCyc; SENT99287:STM4007-MONOMER; -. DR BRENDA; 6.3.1.2; 5542. DR EvolutionaryTrace; P0A1P6; -. DR PHI-base; PHI:7742; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0004356; F:glutamine synthetase activity; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0006542; P:glutamine biosynthetic process; IDA:UniProtKB. DR GO; GO:0019740; P:nitrogen utilization; IDA:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..469 FT /note="Glutamine synthetase" FT /id="PRO_0000153253" 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="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:11329256, FT ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:8099447, FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:2GLS, FT ECO:0007744|PDB:2LGS" FT BINDING 132 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:11329256, FT ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447, FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR, FT ECO:0007744|PDB:2LGS" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:7727369, FT ECO:0007744|PDB:1LGR" FT BINDING 213 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:11329256, FT ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447, FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR, FT ECO:0007744|PDB:2LGS" FT BINDING 221 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:11329256, FT ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447, FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR, FT ECO:0007744|PDB:2LGS" FT BINDING 265..266 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:7727369, FT ECO:0000269|PubMed:8099447, ECO:0000305|PubMed:11329256, FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1FPY, FT ECO:0007744|PDB:1LGR, ECO:0007744|PDB:2LGS" FT BINDING 266 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 270 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:11329256, FT ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:8099447, FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, FT ECO:0007744|PDB:1FPY, ECO:0007744|PDB:2GLS, FT ECO:0007744|PDB:2LGS" FT BINDING 272..274 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:11329256, FT ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, FT ECO:0007744|PDB:1FPY" 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:0000269|PubMed:8099447, FT ECO:0000305|PubMed:11329256, ECO:0007744|PDB:1FPY, FT ECO:0007744|PDB:2LGS" FT BINDING 328 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000305|PubMed:11329256, FT ECO:0007744|PDB:1FPY" 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="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:11329256, FT ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, FT ECO:0000269|PubMed:8099447, ECO:0007744|PDB:1F1H, FT ECO:0007744|PDB:1F52, ECO:0007744|PDB:1FPY, FT ECO:0007744|PDB:1LGR, ECO:0007744|PDB:2GLS, FT ECO:0007744|PDB:2LGS" FT BINDING 360 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:8099447, FT ECO:0007744|PDB:2LGS" FT MOD_RES 398 FT /note="O-AMP-tyrosine" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT CONFLICT 223 FT /note="A -> R (in Ref. 3; CAA59423)" FT /evidence="ECO:0000305" FT CONFLICT 392 FT /note="A -> P (in Ref. 1; AAA27134 and 3; CAA59423)" FT /evidence="ECO:0000305" FT CONFLICT 448 FT /note="R -> P (in Ref. 1; AAA27134)" FT /evidence="ECO:0000305" FT HELIX 3..12 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 17..23 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:1FPY" FT STRAND 29..35 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 41..46 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:1F1H" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:1FPY" FT STRAND 65..70 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:2GLS" FT STRAND 85..93 FT /evidence="ECO:0007829|PDB:1F52" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 105..118 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 123..144 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 147..153 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 158..162 FT /evidence="ECO:0007829|PDB:1F52" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:1FPY" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:1F52" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:1LGR" FT HELIX 190..202 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:1F52" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 219..224 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 229..249 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 260..264 FT /evidence="ECO:0007829|PDB:1FPY" FT STRAND 269..277 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:1F1H" FT HELIX 288..290 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 293..304 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 306..313 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 317..321 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:1F1H" FT STRAND 332..338 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 342..345 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 352..354 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 368..384 FT /evidence="ECO:0007829|PDB:1F52" FT STRAND 398..400 FT /evidence="ECO:0007829|PDB:1F52" FT TURN 403..407 FT /evidence="ECO:0007829|PDB:2GLS" FT HELIX 415..424 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 427..430 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 437..456 FT /evidence="ECO:0007829|PDB:1F52" FT HELIX 460..466 FT /evidence="ECO:0007829|PDB:1F52" SQ SEQUENCE 469 AA; 51786 MW; CD4303E758871E10 CRC64; MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF DGSSIGGWKG INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG YDRDPRSIAK RAEDYLRATG IADTVLFGPE PEFFLFDDIR FGASISGSHV AIDDIEGAWN SSTKYEGGNK GHRPGVKGGY FPVPPVDSAQ DIRSEMCLVM EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK YVVHNVAHRF GKTATFMPKP MFGDNGSGMH CHMSLAKNGT NLFSGDKYAG LSEQALYYIG GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVA SPKARRIEVR FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL PPEEAKEIPQ VAGSLEEALN ALDLDREFLK AGGVFTDEAI DAYIALRREE DDRVRMTPHP VEFELYYSV //