GLN1A_BACSU
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 03-AUG-2022, entry version 170.
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; Firmicutes; 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}.
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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; P12425; -.
DR PRIDE; P12425; -.
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 OMA; PHPHEFE; -.
DR PhylomeDB; P12425; -.
DR BioCyc; BSUB:BSU17460-MON; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0070406; F:glutamine binding; IDA:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 transcription, DNA-templated; IDA:CAFA.
DR GO; GO:0090295; P:nitrogen catabolite repression of transcription; IDA:CAFA.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
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 Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR00653; GlnA; 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 amtB-
FT 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 amtB-
FT lacZ fusion and glnRA-lacZ fusion. Although it is defective
FT in regulation, this mutant retains enzymatic specific
FT activity and similar affinity for ATP, glutamate and
FT 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
