ID   GLN1B_SYNY3             Reviewed;         473 AA.
AC   P77961; Q59981;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1973929};
DE            Short=GS {ECO:0000303|PubMed:1973929};
DE            EC=6.3.1.2 {ECO:0000305|PubMed:1973929};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Glutamine synthetase I beta {ECO:0000305};
DE            Short=GSI beta {ECO:0000305};
GN   Name=glnA {ECO:0000303|PubMed:1973929}; OrderedLocusNames=slr1756;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=7727755; DOI=10.1007/bf00020231;
RA   Reyes J.C., Florencio F.J.;
RT   "Electron transport controls transcription of the glutamine synthetase gene
RT   (glnA) from the cyanobacterium Synechocystis sp. PCC 6803.";
RL   Plant Mol. Biol. 27:789-799(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=1973929; DOI=10.1128/jb.172.8.4732-4735.1990;
RA   Merida A., Leurentop L., Candau P., Florencio F.J.;
RT   "Purification and properties of glutamine synthetases from the
RT   cyanobacteria Synechocystis sp. strain PCC 6803 and Calothrix sp. strain
RT   PCC 7601.";
RL   J. Bacteriol. 172:4732-4735(1990).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8002575; DOI=10.1128/jb.176.24.7516-7523.1994;
RA   Reyes J.C., Florencio F.J.;
RT   "A mutant lacking the glutamine synthetase gene (glnA) is impaired in the
RT   regulation of the nitrate assimilation system in the cyanobacterium
RT   Synechocystis sp. strain PCC 6803.";
RL   J. Bacteriol. 176:7516-7523(1994).
RN   [5]
RP   INDUCTION.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=9098067; DOI=10.1128/jb.179.8.2678-2689.1997;
RA   Reyes J.C., Muro-Pastor M.I., Florencio F.J.;
RT   "Transcription of glutamine synthetase genes (glnA and glnN) from the
RT   cyanobacterium Synechocystis sp. strain PCC 6803 is differently regulated
RT   in response to nitrogen availability.";
RL   J. Bacteriol. 179:2678-2689(1997).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND 2
RP   MANGANESE IONS, AND COFACTOR.
RA   Saelices L., Cascio D., Florencio F.J., Muro-Pastor M.I.;
RT   "Crystal structure of glutamine synthetase from Synechocystis sp. PCC
RT   6803.";
RL   Submitted (JUN-2010) to the PDB data bank.
CC   -!- FUNCTION: Involved in nitrogen metabolism via ammonium assimilation
CC       (PubMed:8002575). Catalyzes the ATP-dependent biosynthesis of glutamine
CC       from glutamate and ammonia (PubMed:1973929, PubMed:8002575).
CC       {ECO:0000269|PubMed:1973929, ECO:0000269|PubMed:8002575}.
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:0000305|PubMed:1973929};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:1973929, ECO:0000269|Ref.6};
CC       Note=Binds 2 Mg(2+) ions per subunit (Ref.6). Also able to bind Co(2+),
CC       Mn(2+) and Ca(2+) ion (PubMed:1973929). {ECO:0000269|PubMed:1973929,
CC       ECO:0000269|Ref.6};
CC   -!- ACTIVITY REGULATION: Inhibited by ADP (90%), AMP (80%), alanine (52%)
CC       and aspartate (41%) (PubMed:1973929). The activity of this enzyme could
CC       be controlled by adenylation under conditions of abundant glutamine (By
CC       similarity). {ECO:0000250|UniProtKB:Q3V5W6,
CC       ECO:0000269|PubMed:1973929}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.17 mM for ammonium {ECO:0000269|PubMed:1973929};
CC         KM=0.55 mM for ATP {ECO:0000269|PubMed:1973929};
CC         KM=1.2 mM for L-glutamate {ECO:0000269|PubMed:1973929};
CC         KM=14.3 mM for L-glutamine {ECO:0000269|PubMed:1973929};
CC         KM=14.5 mM for hydroxylamine {ECO:0000269|PubMed:1973929};
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:1973929};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:1973929};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC       {ECO:0000269|PubMed:1973929}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- INDUCTION: Highly expressed in nitrate- or ammonium-grown cells and
CC       exhibits two- to fourfold-higher expression in nitrogen-starved cells.
CC       {ECO:0000269|PubMed:9098067}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are able to grow with
CC       nitrate as the sole nitrogen source, but are unable to grow in
CC       ammonium-containing medium. This mutant is impaired in the regulation
CC       of the nitrate assimilation system. {ECO:0000269|PubMed:8002575}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {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; X69199; CAA49139.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA17055.1; -; Genomic_DNA.
DR   PIR; S75141; S75141.
DR   PDB; 3NG0; X-ray; 2.80 A; A=1-473.
DR   PDBsum; 3NG0; -.
DR   AlphaFoldDB; P77961; -.
DR   SMR; P77961; -.
DR   DIP; DIP-48822N; -.
DR   IntAct; P77961; 5.
DR   STRING; 1148.gene:10497916; -.
DR   PaxDb; 1148-1652131; -.
DR   EnsemblBacteria; BAA17055; BAA17055; BAA17055.
DR   KEGG; syn:slr1756; -.
DR   eggNOG; COG0174; Bacteria.
DR   InParanoid; P77961; -.
DR   PhylomeDB; P77961; -.
DR   BRENDA; 6.3.1.2; 382.
DR   Proteomes; UP000001425; 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:0019676; P:ammonia assimilation cycle; TAS:GO_Central.
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; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..473
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153272"
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="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
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:0000305|Ref.6, ECO:0007744|PDB:3NG0"
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:0000305|Ref.6, ECO:0007744|PDB:3NG0"
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:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT   BINDING         356
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0"
FT   BINDING         361
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0"
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        115
FT                   /note="V -> A (in Ref. 2; BAA17055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145..147
FT                   /note="QTE -> PNG (in Ref. 1; CAA49139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="Q -> E (in Ref. 1; CAA49139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204..206
FT                   /note="GLC -> AFG (in Ref. 2; BAA17055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="K -> KFDK (in Ref. 1; CAA49139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239
FT                   /note="M -> I (in Ref. 1; CAA49139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="K -> N (in Ref. 1; CAA49139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378..379
FT                   /note="ML -> IV (in Ref. 1; CAA49139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430
FT                   /note="E -> Q (in Ref. 1; CAA49139)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          31..37
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          87..95
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           107..120
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          125..133
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          135..145
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          150..155
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           192..204
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           231..251
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          271..279
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          286..289
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           290..292
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           295..315
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           321..324
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   TURN            327..329
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          337..340
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          344..348
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           355..357
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           371..388
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           418..427
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           430..433
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   STRAND          436..438
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           440..453
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           455..460
FT                   /evidence="ECO:0007829|PDB:3NG0"
FT   HELIX           465..470
FT                   /evidence="ECO:0007829|PDB:3NG0"
SQ   SEQUENCE   473 AA;  53026 MW;  75F8E28EB5EA9515 CRC64;
     MARTPQEVLK WIQDENIKII DLKFIDTPGI WQHCSFYYDQ LDENSFTEGI PFDGSSIRGW
     KAINESDMCM VPDPNTATID PFCKEPTLSM ICSIKEPRTG EWYNRDPRTI AAKAVEYLRG
     TGIADTVYFG PEAEFFLFDD IRFGQTENSS YYFADSVEGR WNTGREEEGG NLGYKPGYKQ
     GYFPVAPTDT AQDIRTEMLL TMAGLCVPIE KHHHEVASGG QNELGIKFDK LVNSADNLMI
     YKYVIKNVAK KYGKTVTFMP KPIFNDNGSG MHVHQSLWKD GQPLFAGDKY AGFSQMGLWY
     IGGILKHAPA LLAFTNPTTN SYKRLVPGFE APVNLAYSQG NRSASVRIPL SGGNPKAKRL
     EFRCPDATSN PYLAFAAMLC AGIDGIKNQI DPGEPLDVDI YDLSPEELAK IPSTPGSLEA
     ALEALEKDHE FLTGTGVFSP DFVESWIEYK LDNEVNPMRL RPHPYEFSLY YDC
//