ID   GLN1B_HELPY             Reviewed;         481 AA.
AC   P94845;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 132.
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=HP_0512;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 367-481.
RC   STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RA   Clairoux N., Boissinot M.;
RT   "Sequence of the dihydrodipicolinate reductase gene (dapB) from
RT   Helicobacter pylori and complementation in Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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}.
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; AE000511; AAD07575.1; -; Genomic_DNA.
DR   EMBL; U75328; AAB39719.1; -; Genomic_DNA.
DR   PIR; H64583; H64583.
DR   RefSeq; NP_207309.1; NC_000915.1.
DR   RefSeq; WP_000637150.1; NC_018939.1.
DR   PDB; 5ZLI; X-ray; 2.80 A; A/B/C/D/E/F=1-481.
DR   PDB; 5ZLP; X-ray; 2.93 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481.
DR   PDBsum; 5ZLI; -.
DR   PDBsum; 5ZLP; -.
DR   AlphaFoldDB; P94845; -.
DR   SMR; P94845; -.
DR   DIP; DIP-3543N; -.
DR   IntAct; P94845; 14.
DR   MINT; P94845; -.
DR   STRING; 85962.HP_0512; -.
DR   PaxDb; 85962-C694_02630; -.
DR   EnsemblBacteria; AAD07575; AAD07575; HP_0512.
DR   KEGG; hpy:HP_0512; -.
DR   PATRIC; fig|85962.47.peg.550; -.
DR   eggNOG; COG0174; Bacteria.
DR   InParanoid; P94845; -.
DR   OrthoDB; 9807095at2; -.
DR   PhylomeDB; P94845; -.
DR   Proteomes; UP000000429; 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   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; 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; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153239"
FT   DOMAIN          22..106
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          114..481
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         274..275
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         275
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         281..283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         331
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         337
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         349
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         349
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         354
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         367
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         369
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   CONFLICT        396
FT                   /note="I -> M (in Ref. 2; AAB39719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="S -> G (in Ref. 2; AAB39719)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..21
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           51..55
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          94..103
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   TURN            104..107
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           114..128
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          142..153
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          156..162
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           200..212
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          217..222
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           238..258
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          278..286
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          295..297
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           302..313
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           315..322
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           326..331
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          349..355
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   TURN            361..363
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          373..375
FT                   /evidence="ECO:0007829|PDB:5ZLP"
FT   HELIX           377..393
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   STRAND          406..409
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           411..416
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           426..434
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           438..441
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           442..444
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           448..461
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           463..466
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   HELIX           472..477
FT                   /evidence="ECO:0007829|PDB:5ZLI"
FT   TURN            478..480
FT                   /evidence="ECO:0007829|PDB:5ZLI"
SQ   SEQUENCE   481 AA;  54514 MW;  87EDFEB540723D3E CRC64;
     MIVRTQNSES KIKEFFEFCK ENEVEFVDFR FSDIKGTWNH IAYSFGALTH GMLKEGIPFD
     ASCFKGWQGI EHSDMILTPD LVRYFIDPFS ADVSVVVFCD VYDVYKNQPY EKCPRSIAKK
     ALQHLKDSGL GDVAYFGAEN EFFIFDSIKI KDASNSQYYE VDSEEGEWNR DRSFENGVNF
     GHRPGKQGGY MPVPPTDTMM DIRTEIVKVL NQVGLETFVV HHEVAQAQGE VGVKFGDLVE
     AADNVQKLKY VVKMVAHLNG KTATFMPKPL YGDNGSGMHT HVSVWKNNEN LFSGETYKGL
     SEFALHFLGG VLRHARGLAA FTNASTNSYK RLIPGYEAPS ILTYSANNRS ASVRIPYGIS
     KNSARFEFRF PDSSSNPYLA FAAILMAGMD GVKNKIDPGE AMDINLFKLT LDEIREKGIK
     QMPHTLRRSL EEMLADKQYL KESQVFSEEF IQAYQSLKFN AEVFPWESKP HPFEFITTYS
     C
//