GLN1A_CLOSA
ID GLN1A_CLOSA Reviewed; 443 AA.
AC P10656;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2891680};
DE Short=GS {ECO:0000303|PubMed:2891680};
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:2891680};
OS Clostridium saccharobutylicum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=169679;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-117 / DSM 13864 / NCP 262;
RX PubMed=2891680; DOI=10.1128/jb.170.1.400-408.1988;
RA Janssen P.J., Jones W.A., Jones D.T., Woods D.R.;
RT "Molecular analysis and regulation of the glnA gene of the Gram-positive
RT anaerobe Clostridium acetobutylicum.";
RL J. Bacteriol. 170:400-408(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RX PubMed=1981087; DOI=10.1111/j.1365-2958.1990.tb02069.x;
RA Janssen P.J., Jones D.T., Woods D.R.;
RT "Studies on Clostridium acetobutylicum glnA promoters and antisense RNA.";
RL Mol. Microbiol. 4:1575-1583(1990).
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.
CC {ECO:0000255|PROSITE-ProRule:PRU01330}.
CC -!- CAUTION: Was originally thought to originate from C.acetobutylicum.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the tyrosine conserved in bacteria and other archaea,
CC involved in feedback inhibition. {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; M18966; AAA23241.1; -; Genomic_DNA.
DR PIR; A28676; AJCLQA.
DR AlphaFoldDB; P10656; -.
DR SMR; P10656; -.
DR STRING; 169679.CSACC_11560; -.
DR PRIDE; P10656; -.
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..443
FT /note="Glutamine synthetase"
FT /id="PRO_0000153234"
FT DOMAIN 16..101
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 108..443
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 239..240
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 240
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 297
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 303
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 315
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 334
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 443 AA; 49682 MW; EDE5BF44495151FC CRC64;
MAKYTKEDII NLVKENGVKF IRLQFTDIFG TLKNVAITDK QLEKALDNEC MFDGSSIDGF
VRIEESDMNL RPNLDSFVIF PWRPQQGKVA RLICDVYKPD GTPFEGDPRH VLKRANADAK
ELGYTMNVGP ECEFFLFETD ENGRATTNTQ DKAGYFDLAP TDLGENARRD MTLALEEMGF
EIEASHHEVA EGQNEIDFKY GDALTTADNI MTFKLVVKSI AQRHGLHASF MPKPIFGING
SGMHVNMSLF KDGKNAFVDE NDKNGLSKVA YQFIAGLLKN IKGMAAVTNP LVNSYKRLVP
GYEAPVYLAW SCKNRTALIR VPAARGAGTR VELRCPDPSS NPYLVLACLL QAGLDGIKNN
LQPPAEVEAN IFAMTEQERK ENGIDNLPNN LYEAVNYMKE NELAKKALGD HVYGNYVAGK
AAEWDDYRTK VHDWELENYL NKY
