ID GLN1A_BACSU Reviewed; 444 AA. AC P12425; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 178. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2906311}; DE Short=GS {ECO:0000303|PubMed:2906311}; DE EC=6.3.1.2 {ECO:0000269|PubMed:12139611, ECO:0000269|PubMed:24158439}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; DE AltName: Full=Glutamine synthetase I alpha {ECO:0000305}; DE Short=GSI alpha {ECO:0000305}; GN Name=glnA {ECO:0000303|PubMed:2906311}; OrderedLocusNames=BSU17460; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2906311; DOI=10.1016/0378-1119(88)90042-x; RA Strauch M.A., Aronson A.I., Brown S.W., Schreier H.J., Sonenshein A.L.; RT "Sequence of the Bacillus subtilis glutamine synthetase gene region."; RL Gene 71:257-265(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. RC STRAIN=ATCC 6633 / PCI 219 / NRS 231; RX PubMed=2565853; DOI=10.1016/0378-1097(89)90151-1; RA Nakano Y., Tanaka E., Kato C., Kimura K., Horikoshi K.; RT "The complete nucleotide sequence of the glutamine synthetase gene (glnA) RT of Bacillus subtilis."; RL FEMS Microbiol. Lett. 48:81-86(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.; RT "Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of RT spoVJ."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [5] RP ACTIVITY REGULATION. RX PubMed=4149044; DOI=10.1016/s0021-9258(19)43119-0; RA Deuel T.F., Prusiner S.; RT "Regulation of glutamine synthetase from Bacillus subtilis by divalent RT cations, feedback inhibitors, and L-glutamine."; RL J. Biol. Chem. 249:257-264(1974). RN [6] RP INDUCTION. RX PubMed=2573733; DOI=10.1016/0022-2836(89)90290-8; RA Schreier H.J., Brown S.W., Hirschi K.D., Nomellini J.F., Sonenshein A.L.; RT "Regulation of Bacillus subtilis glutamine synthetase gene expression by RT the product of the glnR gene."; RL J. Mol. Biol. 210:51-63(1989). RN [7] RP MUTAGENESIS OF VAL-190, AND ACTIVITY REGULATION. RX PubMed=8093698; DOI=10.1128/jb.175.3.892-897.1993; RA Schreier H.J., Rostkowski C.A., Kellner E.M.; RT "Altered regulation of the glnRA operon in a Bacillus subtilis mutant that RT produces methionine sulfoximine-tolerant glutamine synthetase."; RL J. Bacteriol. 175:892-897(1993). RN [8] RP DISRUPTION PHENOTYPE, AND INDUCTION. RC STRAIN=168; RX PubMed=8799114; DOI=10.1073/pnas.93.17.8841; RA Wray L.V. Jr., Ferson A.E., Rohrer K., Fisher S.H.; RT "TnrA, a transcription factor required for global nitrogen regulation in RT Bacillus subtilis."; RL Proc. Natl. Acad. Sci. U.S.A. 93:8841-8845(1996). RN [9] RP FUNCTION, INTERACTION WITH TNRA, AND SUBUNIT. RX PubMed=11719184; DOI=10.1016/s0092-8674(01)00572-4; RA Wray L.V. Jr., Zalieckas J.M., Fisher S.H.; RT "Bacillus subtilis glutamine synthetase controls gene expression through a RT protein-protein interaction with transcription factor TnrA."; RL Cell 107:427-435(2001). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF GLY-59; VAL-190; GLY-302; PRO-306 AND GLU-424. RX PubMed=12139611; DOI=10.1046/j.1365-2958.2002.03054.x; RA Fisher S.H., Brandenburg J.L., Wray L.V. Jr.; RT "Mutations in Bacillus subtilis glutamine synthetase that block its RT interaction with transcription factor TnrA."; RL Mol. Microbiol. 45:627-635(2002). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=17001076; DOI=10.1074/jbc.m607582200; RA Heinrich A., Woyda K., Brauburger K., Meiss G., Detsch C., Stuelke J., RA Forchhammer K.; RT "Interaction of the membrane-bound GlnK-AmtB complex with the master RT regulator of nitrogen metabolism TnrA in Bacillus subtilis."; RL J. Biol. Chem. 281:34909-34917(2006). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 2-444 IN COMPLEX WITH SUBSTRATE RP ANALOG AND 2 MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-62 AND GLU-304, ACTIVITY RP REGULATION, COFACTOR, AND SUBUNIT. RX PubMed=24158439; DOI=10.1074/jbc.m113.519496; RA Murray D.S., Chinnam N., Tonthat N.K., Whitfill T., Wray L.V. Jr., RA Fisher S.H., Schumacher M.A.; RT "Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal RT large intersubunit catalytic conformational changes linked to a unique RT feedback inhibition mechanism."; RL J. Biol. Chem. 288:35801-35811(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND RP 2 MAGNESIUM IONS, FUNCTION, INTERACTION WITH TNRA, MUTAGENESIS OF GLU-424, RP COFACTOR, AND SUBUNIT. RX PubMed=25691471; DOI=10.1101/gad.254714.114; RA Schumacher M.A., Chinnam N.B., Cuthbert B., Tonthat N.K., Whitfill T.; RT "Structures of regulatory machinery reveal novel molecular mechanisms RT controlling B. subtilis nitrogen homeostasis."; RL Genes Dev. 29:451-464(2015). CC -!- FUNCTION: Glutamine synthetase (GS) is an unusual multitasking protein CC that functions as an enzyme, a transcription coregulator, and a CC chaperone in ammonium assimilation and in the regulation of genes CC involved in nitrogen metabolism (PubMed:25691471). It catalyzes the CC ATP-dependent biosynthesis of glutamine from glutamate and ammonia CC (PubMed:24158439). Feedback-inhibited GlnA interacts with and regulates CC the activity of the transcriptional regulator TnrA (PubMed:11719184, CC PubMed:12139611). During nitrogen limitation, TnrA is in its DNA- CC binding active state and turns on the transcription of genes required CC for nitrogen assimilation (PubMed:11719184, PubMed:12139611, CC PubMed:25691471). Under conditions of nitrogen excess, feedback- CC inhibited GlnA forms a stable complex with TnrA, which inhibits its CC DNA-binding activity (PubMed:11719184, PubMed:12139611, CC PubMed:25691471). In contrast, feedback-inhibited GlnA acts as a CC chaperone to stabilize the DNA-binding activity of GlnR, which CC represses the transcription of nitrogen assimilation genes CC (PubMed:25691471). {ECO:0000269|PubMed:11719184, CC ECO:0000269|PubMed:12139611, ECO:0000269|PubMed:24158439, CC ECO:0000269|PubMed:25691471}. 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:0000269|PubMed:12139611, ECO:0000269|PubMed:24158439}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:24158439, ECO:0000269|PubMed:25691471}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:24158439, CC ECO:0000269|PubMed:25691471}; CC -!- ACTIVITY REGULATION: Completely inhibited by glutamine and partially CC inhibited by glycine, alanine and AMP (PubMed:4149044, CC PubMed:24158439). Also inhibited by L-methionine-SR-sulphoximine (Met- CC Sox) (PubMed:8093698, PubMed:24158439). {ECO:0000269|PubMed:24158439, CC ECO:0000269|PubMed:4149044, ECO:0000269|PubMed:8093698}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.18 mM for ammonium {ECO:0000269|PubMed:24158439}; CC KM=0.83 mM for hydroxylamine {ECO:0000269|PubMed:24158439}; CC KM=2.3 mM for ATP {ECO:0000269|PubMed:12139611}; CC KM=2.4 mM for ATP {ECO:0000269|PubMed:24158439}; CC KM=12 mM for glutamine {ECO:0000269|PubMed:12139611}; CC KM=24 mM for glutamate {ECO:0000269|PubMed:12139611}; CC KM=27 mM for glutamate {ECO:0000269|PubMed:24158439}; CC Vmax=3.7 umol/min/mg enzyme {ECO:0000269|PubMed:24158439}; CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons. CC In its feedback-inhibited form, interacts with TnrA in order to block CC its DNA-binding activity. This inhibitory effect is the highest when CC both glutamine and AMP are present. {ECO:0000269|PubMed:11719184, CC ECO:0000269|PubMed:24158439, ECO:0000269|PubMed:25691471}. CC -!- INTERACTION: CC P12425; P37582: glnR; NbExp=3; IntAct=EBI-6402863, EBI-6402856; CC P12425; Q45666: tnrA; NbExp=8; IntAct=EBI-6402863, EBI-8507041; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17001076}. CC -!- INDUCTION: Repressed by GlnR under conditions of nitrogen excess CC (PubMed:2573733). Repressed by TnrA under conditions of nitrogen CC limitation. {ECO:0000269|PubMed:2573733, ECO:0000269|PubMed:8799114}. CC -!- DISRUPTION PHENOTYPE: In cells lacking this gene, expression of glnR, CC tnrA, nasB, nrgAB, gabP and ure genes is derepressed. CC {ECO:0000269|PubMed:8799114}. 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; M22811; AAA83376.1; -; Genomic_DNA. DR EMBL; D00854; BAA00730.1; -; Genomic_DNA. DR EMBL; U66480; AAB41080.1; -; Genomic_DNA. DR EMBL; AL009126; CAB13630.1; -; Genomic_DNA. DR PIR; JT0392; AJBSQS. DR RefSeq; NP_389628.1; NC_000964.3. DR RefSeq; WP_003231737.1; NZ_JNCM01000035.1. DR PDB; 4LNF; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=2-444. DR PDB; 4LNI; X-ray; 2.58 A; A/B/C/D/E/F/G/H/I/J/K/L=2-444. DR PDB; 4LNK; X-ray; 2.87 A; A/B/C/D/E/F=2-444. DR PDB; 4LNN; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=2-444. DR PDB; 4LNO; X-ray; 2.90 A; A/B/C/D/E/F=2-444. DR PDB; 4S0R; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-444. DR PDBsum; 4LNF; -. DR PDBsum; 4LNI; -. DR PDBsum; 4LNK; -. DR PDBsum; 4LNN; -. DR PDBsum; 4LNO; -. DR PDBsum; 4S0R; -. DR AlphaFoldDB; P12425; -. DR SMR; P12425; -. DR DIP; DIP-29670N; -. DR IntAct; P12425; 4. DR MINT; P12425; -. DR STRING; 224308.BSU17460; -. DR MoonProt; P12425; -. DR jPOST; P12425; -. DR PaxDb; 224308-BSU17460; -. DR EnsemblBacteria; CAB13630; CAB13630; BSU_17460. DR GeneID; 940020; -. DR KEGG; bsu:BSU17460; -. DR PATRIC; fig|224308.179.peg.1894; -. DR eggNOG; COG0174; Bacteria. DR InParanoid; P12425; -. DR OrthoDB; 9807095at2; -. DR PhylomeDB; P12425; -. DR BioCyc; BSUB:BSU17460-MONOMER; -. DR BRENDA; 6.3.1.2; 658. DR SABIO-RK; P12425; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA. DR GO; GO:0016595; F:glutamate binding; IDA:UniProtKB. DR GO; GO:0070406; F:glutamine binding; IDA:CAFA. DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0043562; P:cellular response to nitrogen levels; IDA:CAFA. DR GO; GO:0006542; P:glutamine biosynthetic process; IMP:CACAO. DR GO; GO:1904797; P:negative regulation of core promoter binding; IDA:CAFA. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:CAFA. DR GO; GO:0090295; P:nitrogen catabolite repression of transcription; IDA:CAFA. 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; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1. DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 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; Direct protein sequencing; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2565853" FT CHAIN 2..444 FT /note="Glutamine synthetase" FT /id="PRO_0000153233" FT DOMAIN 16..101 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 108..444 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="1" FT /evidence="ECO:0000269|PubMed:24158439, FT ECO:0000269|PubMed:25691471, ECO:0007744|PDB:4LNF, FT ECO:0007744|PDB:4LNI, ECO:0007744|PDB:4LNK, FT ECO:0007744|PDB:4LNN, ECO:0007744|PDB:4S0R" FT BINDING 134 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24158439, FT ECO:0000269|PubMed:25691471, ECO:0007744|PDB:4LNF, FT ECO:0007744|PDB:4LNI, ECO:0007744|PDB:4LNK, FT ECO:0007744|PDB:4S0R" FT BINDING 184 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 189 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24158439, FT ECO:0000269|PubMed:25691471, ECO:0007744|PDB:4LNF, FT ECO:0007744|PDB:4LNI, ECO:0007744|PDB:4LNK, FT ECO:0007744|PDB:4S0R" FT BINDING 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24158439, FT ECO:0000269|PubMed:25691471, ECO:0007744|PDB:4LNF, FT ECO:0007744|PDB:4LNI, ECO:0007744|PDB:4LNK, FT ECO:0007744|PDB:4S0R" FT BINDING 240..241 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 241 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:24158439, FT ECO:0000269|PubMed:25691471, ECO:0007744|PDB:4LNF, FT ECO:0007744|PDB:4LNK, ECO:0007744|PDB:4LNN, FT ECO:0007744|PDB:4S0R" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24158439, FT ECO:0000269|PubMed:25691471, ECO:0007744|PDB:4LNF, FT ECO:0007744|PDB:4LNK, ECO:0007744|PDB:4S0R" FT BINDING 249 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 298 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 304 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 316 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 316 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 321 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 333 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24158439, FT ECO:0000269|PubMed:25691471, ECO:0007744|PDB:4LNF, FT ECO:0007744|PDB:4LNI, ECO:0007744|PDB:4LNK, FT ECO:0007744|PDB:4LNN, ECO:0007744|PDB:4S0R" FT BINDING 335 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT SITE 62 FT /note="Important for inhibition by glutamine" FT /evidence="ECO:0000269|PubMed:24158439" FT VARIANT 10 FT /note="E -> V (in strain: PCI 219)" FT VARIANT 43 FT /note="G -> E (in strain: PCI 219)" FT VARIANT 253 FT /note="N -> D (in strain: PCI 219)" FT VARIANT 259 FT /note="F -> Y (in strain: PCI 219)" FT MUTAGEN 59 FT /note="G->R: Unable to form stable complex with TnrA. In FT the presence of glutamine, this mutant derepresses FT amtB-lacZ fusion and glnRA-lacZ fusion." FT /evidence="ECO:0000269|PubMed:12139611" FT MUTAGEN 62 FT /note="R->A: Highly resistant to inhibition by glutamine FT and AMP. Regulation by TnrA and GlnR is abolished. Only FT small differences (less than 2-fold) in its steady-state FT kinetic constants compared with the wild-type. Similar FT sensitivity to Met-Sox that compared to the wild-ytpe." FT /evidence="ECO:0000269|PubMed:24158439" FT MUTAGEN 190 FT /note="V->A: Unable to form stable complex with TnrA. In FT the presence of glutamine, this mutant partially relieves FT expression of the glnRA-lacZ fusion, but has no effect on FT the TnrA-dependent regulation of amtB-lacZ fusion. FT Resistant to inhibition by MetSox." FT /evidence="ECO:0000269|PubMed:12139611, FT ECO:0000269|PubMed:8093698" FT MUTAGEN 302 FT /note="G->E: Unable to form stable complex with TnrA. In FT the presence of glutamine, amtB-lacZ fusion is only 4-fold FT regulated by TnrA, whereas glnRA-lacZ fusion is FT derepressed. This mutant retains enzymatic specific FT activity with a 2-fold decrease of the affinity for FT glutamate and glutamine compared to the wild-type. Slightly FT less sensitive to inhibition by glutamine." FT /evidence="ECO:0000269|PubMed:12139611" FT MUTAGEN 304 FT /note="E->A: Highly resistant to Met-Sox inhibition. 8- and FT 2-fold increase of the affinity for glutamate and ATP, FT respectively. Strong decrease of the affinity for FT ammonium." FT /evidence="ECO:0000269|PubMed:24158439" FT MUTAGEN 306 FT /note="P->H: Unable to form stable complex with TnrA. In FT the presence of glutamine, this mutant completely FT derepresses glnRA-lacZ fusion, whereas amtB-lacZ fusion FT expression is only partially derepresses." FT /evidence="ECO:0000269|PubMed:12139611" FT MUTAGEN 424 FT /note="E->K: Unable to form stable complex with TnrA. In FT the presence of glutamine, this mutant derepresses FT amtB-lacZ fusion and glnRA-lacZ fusion. Although it is FT defective in regulation, this mutant retains enzymatic FT specific activity and similar affinity for ATP, glutamate FT and glutamine compared to the wild-type. Slightly less FT sensitive to inhibition by glutamine." FT /evidence="ECO:0000269|PubMed:12139611, FT ECO:0000269|PubMed:25691471" FT HELIX 6..16 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 20..26 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:4S0R" FT STRAND 32..38 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 42..46 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:4S0R" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 67..80 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 89..97 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 99..103 FT /evidence="ECO:0007829|PDB:4LNK" FT HELIX 108..121 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:4LNN" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:4LNI" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:4LNK" FT HELIX 166..178 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 183..188 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 194..199 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 204..224 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 244..252 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:4LNK" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 269..289 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 295..298 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 311..313 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 316..322 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:4LNI" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 343..359 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 377..383 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 392..400 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 403..409 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 411..430 FT /evidence="ECO:0007829|PDB:4LNI" FT HELIX 434..440 FT /evidence="ECO:0007829|PDB:4LNI" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:4LNI" SQ SEQUENCE 444 AA; 50278 MW; 83A5657CE1388AB0 CRC64; MAKYTREDIE KLVKEENVKY IRLQFTDILG TIKNVEIPVS QLGKALDNKV MFDGSSIEGF VRIEESDMYL YPDLNTFVIF PWTAEKGKVA RFICDIYNPD GTPFEGDPRN NLKRILKEME DLGFSDFNLG PEPEFFLFKL DEKGEPTLEL NDKGGYFDLA PTDLGENCRR DIVLELEEMG FEIEASHHEV APGQHEIDFK YAGAVRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLFGVN GSGMHCNLSL FKNGVNAFFD ENADLQLSET AKHFIAGIVK HATSFTAVTN PTVNSYKRLV PGYEAPCYVA WSAQNRSPLI RIPASRGIST RVEVRSVDPA ANPYLALSVL LAAGLDGIKN KLEAPAPIDR NIYVMSKEER MENGIVDLPA TLAEALEEFK SNEVMVKALG EHLFEHFIEA KEIEWDMFRT QVHPWEREQY MSQY //