ID GLN1A_LACDE Reviewed; 445 AA. AC P45627; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1359838}; DE Short=GS {ECO:0000303|PubMed:1359838}; 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:1359838}; OS Lactobacillus delbrueckii subsp. bulgaricus. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1585; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1359838; DOI=10.1128/aem.58.9.3165-3169.1992; RA Ishino Y., Morgenthaler P., Hottinger H., Soell D.; RT "Organization and nucleotide sequence of the glutamine synthetase (glnA) RT gene from Lactobacillus delbrueckii subsp. bulgaricus."; RL Appl. Environ. Microbiol. 58:3165-3169(1992). 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; D10020; BAA00910.1; -; Genomic_DNA. DR PIR; A48947; A48947. DR AlphaFoldDB; P45627; -. DR SMR; P45627; -. 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; 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; 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. FT CHAIN 1..445 FT /note="Glutamine synthetase" FT /id="PRO_0000153241" FT DOMAIN 17..103 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 110..445 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 134 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 136 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 198 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 243 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 247 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 251 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 300 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 306 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT BINDING 318 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 318 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 323 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 335 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 337 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P0A1P6" FT SITE 63 FT /note="Important for inhibition by glutamine" FT /evidence="ECO:0000250|UniProtKB:P12425" SQ SEQUENCE 445 AA; 50134 MW; A57A9E11ABAF87E8 CRC64; MSKVITEEEI RKDVEEKNVR FLRLAFTDIN GTLKNLEVPV SQLDDVLGNQ TRFDGSSIDG FVRLEESDMV LYPDLATWLV LAWTTVEEGT IGRLVCSVHN VDGTPFEGDP RNNLKKVIAE MEEMGFSDFE IGFEAEFFLF KEGKNGEETT KVSDHSSYFD MASEDEGAKC RREIVETLEK LGFRVEAAHH EVGDGQQEID FRFDNALATA DKLQTFKMVV KTIARKYHLH ASFMAKPVEG LAGNGMHTNM SLLKDGKNAF YDKDGQYNLS TTALTFLNGI LEHARAITCV ANPTVNSYKR LIPGFEAPVY ISWASRNRSP MVRIPNANEV GTRLEMRSTD PTANPYLLLS ACLKAGLTGI KEGKLPMAPV TSNLFEMTDD ERKELGIKPL PSTLHNAIKA FKEDEVVKSA FSEHIVDSFL ELKETEWALY TQSVSEWEVK RYFNY //