GLN1A_LACDE
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 03-AUG-2022, entry version 87.
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; Firmicutes; 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}.
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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:glutamate-ammonia ligase 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; -; 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; 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; 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
