ID   GLN1B_PICP2             Reviewed;         473 AA.
AC   P28605; B1XNU5;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P77961};
DE            Short=GS {ECO:0000250|UniProtKB:P77961};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P77961};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P77961};
DE   AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P77961};
DE            Short=GSI beta {ECO:0000250|UniProtKB:P77961};
GN   Name=glnA {ECO:0000250|UniProtKB:P77961};
GN   OrderedLocusNames=SYNPCC7002_A1630;
OS   Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Picosynechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX   PubMed=7678591; DOI=10.1128/jb.175.3.604-612.1993;
RA   Wagner S.J., Thomas S.P., Kaufman R.I., Nixon B.T., Stevens S.E. Jr.;
RT   "The glnA gene of the cyanobacterium Agmenellum quadruplicatum PR-6 is
RT   nonessential for ammonium assimilation.";
RL   J. Bacteriol. 175:604-612(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in nitrogen metabolism via ammonium assimilation.
CC       Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate
CC       and ammonia. {ECO:0000250|UniProtKB:P77961}.
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:P77961};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P77961};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P77961};
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 hexagons.
CC       {ECO:0000250|UniProtKB:P77961}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000250|UniProtKB:P77961}.
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DR   EMBL; Z13965; CAA78366.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACA99620.1; -; Genomic_DNA.
DR   RefSeq; WP_012307243.1; NZ_JAHHPU010000002.1.
DR   AlphaFoldDB; P28605; -.
DR   SMR; P28605; -.
DR   STRING; 32049.SYNPCC7002_A1630; -.
DR   KEGG; syp:SYNPCC7002_A1630; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_017290_1_2_3; -.
DR   Proteomes; UP000001688; 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: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; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR43407:SF1; LENGSIN; 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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..473
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153271"
FT   DOMAIN          15..100
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          107..473
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         267..268
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         268
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         274..276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         324
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         330
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         342
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         356
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         361
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         363
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   MOD_RES         401
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   CONFLICT        120
FT                   /note="A -> P (in Ref. 1; CAA78366)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  53004 MW;  62323C804178884B CRC64;
     MTQTATDVLR LIQEENIQII DLKFVDLPGI WQHCSFYQDQ LDEASFVDGV PFDGSSIRGW
     KAINESDMAM VPDPTTAWID PFCKEKTLSL ICSIKEPRTG EWYSRDPRSI AQKAVDYLAA
     SGIGDTAYFG PEAEFFVFDD VRFDQTENKG FYYVDSVEGR WNSGRKEPGG NLAHKPGYKQ
     GYFPVPPTDT LQDMRTEMLL TMAKCGVPIE KHHHEVATGG QNELGFRFAT LLKAADYLMT
     YKYVIKNVAR KYGRTVTFMP KPLFNDNGSG MHTHQSLWKE GQPLFWGDRY ANLSQLALHY
     IGGILKHAPA LLAFSNPSTN SYKRLVPGFE APVNLAYSQG NRSASVRIPL SGPNPKAKRL
     EFRCPDATAN PYLAFAAMLC AGIDGIKNAI DPGDPLDVDI YDLTPEELSK IPSTPASLEA
     ALEALQQDHD FLTAGGVFTT DFIENWIEYK LDAEVNPLRL RPHPYEFALY YDC
//