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GLN1B_ECOL6
ID   GLN1B_ECOL6             Reviewed;         469 AA.
AC   P0A9C6; P06711;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=c4819;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83248.1; -; Genomic_DNA.
DR   RefSeq; WP_001271717.1; NC_004431.1.
DR   AlphaFoldDB; P0A9C6; -.
DR   SMR; P0A9C6; -.
DR   STRING; 199310.c4819; -.
DR   EnsemblBacteria; AAN83248; AAN83248; c4819.
DR   GeneID; 66672224; -.
DR   KEGG; ecc:c4819; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_017290_1_2_6; -.
DR   OMA; PHPHEFE; -.
DR   BioCyc; ECOL199310:C4819-MON; -.
DR   Proteomes; UP000001410; 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; IPR001637; Gln_synth_I_adenylation_site.
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; PS00182; GLNA_ADENYLATION; 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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..469
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153237"
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:0000250|UniProtKB:P9WN39"
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
 
 
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