ID GLN1A_BACCE Reviewed; 444 AA. AC P19064; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 113. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2572584}; DE Short=GS {ECO:0000303|PubMed:2572584}; DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P12425}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P12425}; DE AltName: Full=Glutamine synthetase I alpha {ECO:0000250|UniProtKB:P12425}; DE Short=GSI alpha {ECO:0000250|UniProtKB:P12425}; GN Name=glnA {ECO:0000303|PubMed:2572584}; OS Bacillus cereus. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19. RC STRAIN=NBRC 3131; RX PubMed=2572584; DOI=10.1093/oxfordjournals.jbchem.a122834; RA Nakano Y., Kato C., Tanaka E., Kimura K., Horikoshi K.; RT "Nucleotide sequence of the glutamine synthetase gene (glnA) and its RT upstream region from Bacillus cereus."; RL J. Biochem. 106:209-215(1989). 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. It catalyzes the ATP-dependent CC biosynthesis of glutamine from glutamate and ammonia. Feedback- CC inhibited GlnA also interacts with and regulates the activity of the CC transcriptional regulator TnrA. During nitrogen limitation, TnrA is in CC its DNA-binding active state and turns on the transcription of genes CC required for nitrogen assimilation. Under conditions of nitrogen CC excess, feedback-inhibited GlnA forms a stable complex with TnrA, which CC inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA CC acts as a chaperone to stabilize the DNA-binding activity of GlnR, CC which represses the transcription of nitrogen assimilation genes. CC {ECO:0000250|UniProtKB:P12425}. 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:P12425}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P12425}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425}; CC -!- ACTIVITY REGULATION: Inhibited by glutamine. CC {ECO:0000250|UniProtKB:P12425}. 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. {ECO:0000250|UniProtKB:P12425}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12425}. 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; D00513; BAA00403.1; -; Genomic_DNA. DR PIR; JU0075; AJBSQU. DR AlphaFoldDB; P19064; -. DR SMR; P19064; -. DR eggNOG; COG0174; Bacteria. 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; 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 ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2572584" FT CHAIN 2..444 FT /note="Glutamine synthetase" FT /id="PRO_0000153232" 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:0000250|UniProtKB:P12425" FT BINDING 134 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" 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:0000250|UniProtKB:P12425" FT BINDING 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" 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:0000250|UniProtKB:P12425" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" 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:0000250|UniProtKB:P12425" 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:0000250|UniProtKB:P12425" SQ SEQUENCE 444 AA; 50195 MW; 75A4A2525A445FF7 CRC64; MARYTKEDIF RLAKEENVKY IRLQFTDLLG VIKNVEIPVS QLTKALDNKM MFDGSSIEGF VRIEESDMYL YPDLDTWVIF PWTAEKGKVA RLICDIYNAD GTPFEGDPRN NLKRVLKEME ALGFSDFNLG PEPEFFLFKV DEKGNPTLEL NDNGGYFDLA PMDLGENCRR DIVLELEEMG FEIEASHHEV APGQHEIDFK YANAIRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLYGVN GSGMHCNLSL FKNGENVFYD QNGDLQLSDD ARHFIAGILK HAPAFTAVAN PTVNSYKRLV PGYEAPCYVA WSAQNRSPLV RIPASRGIST RVEVRSVDPA ANPYLVMATL LAAGLDGIKN KLTPPAAVDR NIYVMTKEER EEAGIVDLPA TLAQALVTLQ SNEVISNALG DHLLEHFIEA KEFEWDIFRT QVHQWERDQY MSLY //