ID   GLN1B_PSEAE             Reviewed;         469 AA.
AC   Q9HU65;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P0A1P6};
DE            Short=GS {ECO:0000250|UniProtKB:P0A1P6};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P0A1P6};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P0A1P6};
DE            Short=GSI beta {ECO:0000250|UniProtKB:P0A1P6};
GN   Name=glnA {ECO:0000250|UniProtKB:P0A1P6}; OrderedLocusNames=PA5119;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 37-59; 118-140; 142-150; 152-170; 178-193; 432-447 AND
RP   456-469.
RC   STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA   Liddor M.;
RT   "Biofouling in water treatment systems: effect of membrane properties on
RT   biofilm formation.";
RL   Thesis (2005), Ben-Gurion University, Israel.
CC   -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC       glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}.
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:P0A1P6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WN39};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39};
CC   -!- ACTIVITY REGULATION: The activity of this enzyme could be controlled by
CC       adenylation under conditions of abundant glutamine.
CC       {ECO:0000250|UniProtKB:Q3V5W6}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric
CC       ring. {ECO:0000250|UniProtKB:P0A1P6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG08504.1; -; Genomic_DNA.
DR   PIR; G83005; G83005.
DR   RefSeq; NP_253806.1; NC_002516.2.
DR   RefSeq; WP_003096016.1; NZ_QZGE01000002.1.
DR   AlphaFoldDB; Q9HU65; -.
DR   SMR; Q9HU65; -.
DR   STRING; 208964.PA5119; -.
DR   PaxDb; 208964-PA5119; -.
DR   GeneID; 77223648; -.
DR   GeneID; 877688; -.
DR   KEGG; pae:PA5119; -.
DR   PATRIC; fig|208964.12.peg.5365; -.
DR   PseudoCAP; PA5119; -.
DR   HOGENOM; CLU_017290_1_2_6; -.
DR   InParanoid; Q9HU65; -.
DR   OrthoDB; 9807095at2; -.
DR   PhylomeDB; Q9HU65; -.
DR   BioCyc; PAER208964:G1FZ6-5234-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019740; P:nitrogen utilization; IBA:GO_Central.
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; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR43407:SF2; GLUTAMINE SYNTHETASE; 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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..469
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153251"
FT   DOMAIN          12..97
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          105..469
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         265..266
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         266
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         272..274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         322
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         328
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         340
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         358
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         360
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   MOD_RES         398
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
SQ   SEQUENCE   469 AA;  51945 MW;  DED83E755B3CD225 CRC64;
     MSYKSHQLIK DHDVKWVDLR FTDTKGKQQH VTMPARDALD DEFFEAGKMF DGSSIAGWKG
     IEASDMILMP DDSTAVLDPF TEEPTLILVC DIIEPSTMQG YERDPRNIAK RAEEYLKSTG
     IGDTVFVGPE PEFFIFDEVK FKSDISGSMF KIFSEQASWN TDADIESGNK GHRPGVKGGY
     FPVPPVDHDH EIRTAMCNAL EEMGLVVEVH HHEVATAGQN EIGVKFNTLV AKADEVQTLK
     YCVHNVADAY GKTVTFMPKP LYGDNGSGMH VHMSISKDGK NTFAGEGYAG LSETALYFIG
     GIIKHGKALN GFTNPSTNSY KRLVPGFEAP VMLAYSARNR SASIRIPYVS SPKARRIEAR
     FPDPAANPYL AFAALLMAGL DGIQNKIHPG DAADKNLYDL PPEEAKEIPQ VCGSLKEALE
     ELDKGRAFLT KGGVFTDEFI DAYIELKSEE EIKVRTFVHP LEYDLYYSV
//