GLN1B_HELPY
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 03-AUG-2022, entry version 123.
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; Proteobacteria; 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}.
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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.C694_02630; -.
DR PaxDb; P94845; -.
DR EnsemblBacteria; AAD07575; AAD07575; HP_0512.
DR KEGG; hpy:HP_0512; -.
DR PATRIC; fig|85962.47.peg.550; -.
DR eggNOG; COG0174; Bacteria.
DR OMA; VFPWESK; -.
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:glutamate-ammonia ligase 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; -; 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 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; 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
