ID   GLN1B_ECOLI             Reviewed;         469 AA.
AC   P0A9C5; P06711; Q2M8G7;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 141.
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};
GN   OrderedLocusNames=b3870, JW3841;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2882477; DOI=10.1093/nar/15.6.2757;
RA   Miranda-Rios J., Sanchez-Pescador R., Urdea M., Covarrubias A.A.;
RT   "The complete nucleotide sequence of the glnALG operon of Escherichia coli
RT   K12.";
RL   Nucleic Acids Res. 15:2757-2770(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2874141; DOI=10.1016/s0021-9258(18)67425-3;
RA   Colombo G., Villafranca J.J.;
RT   "Amino acid sequence of Escherichia coli glutamine synthetase deduced from
RT   the DNA nucleotide sequence.";
RL   J. Biol. Chem. 261:10587-10591(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RX   PubMed=6134228; DOI=10.1007/bf00330342;
RA   Covarrubias A.A., Bastarrachea F.;
RT   "Nucleotide sequence of the glnA control region of Escherichia coli.";
RL   Mol. Gen. Genet. 190:171-175(1983).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX   PubMed=2858855; DOI=10.1073/pnas.82.7.1979;
RA   Reitzer L.J., Magasanik B.;
RT   "Expression of glnA in Escherichia coli is regulated at tandem promoters.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1979-1983(1985).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 363-469.
RX   PubMed=2865194; DOI=10.1016/0378-1119(85)90261-6;
RA   Rocha M., Vazquez M., Garciarrubio A., Covarrubias A.A.;
RT   "Nucleotide sequence of the glnA-glnL intercistronic region of Escherichia
RT   coli.";
RL   Gene 37:91-99(1985).
RN   [10]
RP   PROTEIN SEQUENCE OF 387-406, SEQUENCE REVISION, AND AMPYLATION AT TYR-398.
RX   PubMed=5543675; DOI=10.1016/s0021-9258(18)62436-6;
RA   Heinrikson R.L., Kingdon H.S.;
RT   "Primary structure of Escherichia coli glutamine synthetase. II. The
RT   complete amino acid sequence of a tryptic heneicosapeptide containing
RT   covalently bound adenylic acid.";
RL   J. Biol. Chem. 246:1099-1106(1971).
RN   [11]
RP   PROTEIN SEQUENCE OF 394-406, AND AMPYLATION AT TYR-398.
RX   PubMed=4904088; DOI=10.1016/s0021-9258(18)63431-3;
RA   Heinrikson R.L., Kingdon H.S.;
RT   "The amino acid sequence in the vicinity of the covalently bound adenylic
RT   acid in glutamine synthetase from Escherichia coli.";
RL   J. Biol. Chem. 245:138-142(1970).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-469.
RX   PubMed=6148334; DOI=10.1128/jb.160.1.379-384.1984;
RA   Ueno-Nishio S., Mango S., Reitzer L.J., Magasanik B.;
RT   "Identification and regulation of the glnL operator-promoter of the complex
RT   glnALG operon of Escherichia coli.";
RL   J. Bacteriol. 160:379-384(1984).
RN   [13]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
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   -!- INTERACTION:
CC       P0A9C5; P0A9C5: glnA; NbExp=2; IntAct=EBI-909063, EBI-909063;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X05173; CAA28806.1; -; Genomic_DNA.
DR   EMBL; M13746; AAA23879.1; -; Genomic_DNA.
DR   EMBL; L19201; AAB03004.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76867.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77439.1; -; Genomic_DNA.
DR   EMBL; J01618; AAA98066.1; -; Genomic_DNA.
DR   EMBL; M10421; AAA23882.1; -; Genomic_DNA.
DR   EMBL; K02176; AAA23880.1; -; Genomic_DNA.
DR   PIR; S40815; AJECQ.
DR   RefSeq; NP_418306.1; NC_000913.3.
DR   RefSeq; WP_001271717.1; NZ_STEB01000017.1.
DR   PDB; 7W85; EM; 2.94 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/U/V/W/X/Y=1-469.
DR   PDBsum; 7W85; -.
DR   AlphaFoldDB; P0A9C5; -.
DR   EMDB; EMD-32352; -.
DR   SMR; P0A9C5; -.
DR   BioGRID; 4262630; 46.
DR   BioGRID; 852667; 1.
DR   DIP; DIP-9777N; -.
DR   IntAct; P0A9C5; 10.
DR   STRING; 511145.b3870; -.
DR   BindingDB; P0A9C5; -.
DR   ChEMBL; CHEMBL3789; -.
DR   MetOSite; P0A9C5; -.
DR   jPOST; P0A9C5; -.
DR   PaxDb; 511145-b3870; -.
DR   EnsemblBacteria; AAC76867; AAC76867; b3870.
DR   GeneID; 75204328; -.
DR   GeneID; 948370; -.
DR   KEGG; ecj:JW3841; -.
DR   KEGG; eco:b3870; -.
DR   PATRIC; fig|1411691.4.peg.2841; -.
DR   EchoBASE; EB0378; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_017290_1_2_6; -.
DR   InParanoid; P0A9C5; -.
DR   OMA; PHPHEFE; -.
DR   OrthoDB; 9807095at2; -.
DR   PhylomeDB; P0A9C5; -.
DR   BioCyc; EcoCyc:GLUTAMINESYN-MONOMER; -.
DR   BioCyc; MetaCyc:GLUTAMINESYN-MONOMER; -.
DR   SABIO-RK; P0A9C5; -.
DR   PRO; PR:P0A9C5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019676; P:ammonia assimilation cycle; IDA:EcoCyc.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019740; P:nitrogen utilization; IDA:EcoCyc.
DR   GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
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.
DR   SWISS-2DPAGE; P0A9C5; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298646"
FT   CHAIN           2..469
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153235"
FT   DOMAIN          13..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:0000269|PubMed:4904088,
FT                   ECO:0000269|PubMed:5543675"
FT   CONFLICT        90
FT                   /note="C -> S (in Ref. 2; AAA23879)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108..109
FT                   /note="IA -> MS (in Ref. 2; AAA23879)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="C -> S (in Ref. 2; AAA23879)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228
FT                   /note="T -> I (in Ref. 1; CAA28806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247..248
FT                   /note="AH -> VRN (in Ref. 1; CAA28806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305..306
FT                   /note="HA -> QP (in Ref. 1; CAA28806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        394..395
FT                   /note="DK -> KD (in Ref. 10; AA sequence and 11; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  51904 MW;  0AFC05724CDEBA36 CRC64;
     MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF DGSSIGGWKG
     INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG YDRDPRSIAK RAEDYLRSTG
     IADTVLFGPE PEFFLFDDIR FGSSISGSHV AIDDIEGAWN SSTQYEGGNK GHRPAVKGGY
     FPVPPVDSAQ DIRSEMCLVM EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK
     YVVHNVAHRF GKTATFMPKP MFGDNGSGMH CHMSLSKNGV NLFAGDKYAG LSEQALYYIG
     GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVS SPKARRIEVR
     FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL PPEEAKEIPQ VAGSLEEALN
     ELDLDREFLK AGGVFTDEAI DAYIALRREE DDRVRMTPHP VEFELYYSV
//