GLN1A_STAAR
ID GLN1A_STAAR Reviewed; 446 AA.
AC Q6GHC6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P12425};
DE Short=GS {ECO:0000250|UniProtKB:P12425};
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:0000250|UniProtKB:P12425}; OrderedLocusNames=SAR1284;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40287.1; -; Genomic_DNA.
DR RefSeq; WP_001126604.1; NC_002952.2.
DR AlphaFoldDB; Q6GHC6; -.
DR SMR; Q6GHC6; -.
DR KEGG; sar:SAR1284; -.
DR HOGENOM; CLU_017290_1_3_9; -.
DR OMA; PHPHEFE; -.
DR OrthoDB; 416474at2; -.
DR Proteomes; UP000000596; Chromosome.
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..446
FT /note="Glutamine synthetase"
FT /id="PRO_0000153260"
FT DOMAIN 18..103
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 110..446
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 242..243
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
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 64
FT /note="Important for inhibition by glutamine"
FT /evidence="ECO:0000250|UniProtKB:P12425"
SQ SEQUENCE 446 AA; 50857 MW; 988F5EF566C4C6D4 CRC64;
MPKRTFTKDD IRKFAEEENV RYLRLQFTDI LGTIKNVEVP VSQLEKVLDN EMMFDGSSIE
GFVRIEESDM YLHPDLDTWV IFPWTAGQGK VARLICDVYK TDGTPFEGDP RANLKRVLKE
MEDLGFTDFN LGPEPEFFLF KLDEKGEPTL ELNDDGGYFD LAPTDLGENC RRDIVLELED
MGFDIEASHH EVAPGQHEID FKYADAVTAC DNIQTFKLVV KTIARKHNLH ATFMPKPLFG
VNGSGMHFNV SLFKGKENAF FDPNTEMGLT ETAYQFTAGV LKNARGFTAV CNPLVNSYKR
LVPGYEAPCY IAWSGKNRSP LIRVPSSRGL STRIEVRSVD PAANPYMALA AILESGLDGI
KNKLKVPEPV NQNIYEMNRE EREAVGIQDL PSTLYTALKA MRENEVIKKA LGNHIYNQFI
NSKSIEWDYY RTQVSEWERD QYMKQY
