ID   GLNA2_BRADU             Reviewed;         344 AA.
AC   P04772;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|Ref.1};
DE            Short=GS {ECO:0000303|Ref.1};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P16580};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Glutamine synthetase II {ECO:0000303|Ref.1};
DE            Short=GSII {ECO:0000303|Ref.1};
GN   Name=glnII {ECO:0000303|Ref.1}; OrderedLocusNames=blr4169;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RA   Carlson T.A., Chelm B.K.;
RT   "Apparent eukaryotic origin of glutamine synthetase II from the bacterium
RT   Bradyrhizobium japonicum.";
RL   Nature 322:568-570(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC       glutamate and ammonia. {ECO:0000250|UniProtKB:Q02154}.
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:P16580};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P16580};
CC   -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000250|UniProtKB:Q02154}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16580}.
CC   -!- MISCELLANEOUS: Two forms of glutamine synthetase (GSI and GSII) can be
CC       found in this nitrogen fixing bacteria, GSI is a typical prokaryotic
CC       glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.
CC       {ECO:0000305|Ref.1}.
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; X04187; CAA27779.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC49434.1; -; Genomic_DNA.
DR   PIR; A24155; AJZJQ2.
DR   RefSeq; NP_770809.1; NC_004463.1.
DR   RefSeq; WP_011086942.1; NZ_CP011360.1.
DR   AlphaFoldDB; P04772; -.
DR   SMR; P04772; -.
DR   STRING; 224911.AAV28_17885; -.
DR   EnsemblBacteria; BAC49434; BAC49434; BAC49434.
DR   GeneID; 64023900; -.
DR   KEGG; bja:blr4169; -.
DR   PATRIC; fig|224911.44.peg.3887; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_036762_1_0_5; -.
DR   InParanoid; P04772; -.
DR   OrthoDB; 9807095at2; -.
DR   PhylomeDB; P04772; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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; IPR027302; Gln_synth_N_conserv_site.
DR   PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 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   ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium;
KW   Metal-binding; Nitrogen fixation; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..344
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153220"
FT   DOMAIN          4..86
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          89..344
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         109
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         278
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   CONFLICT        37..38
FT                   /note="QL -> HV (in Ref. 1; CAA27779)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326..344
FT                   /note="ASQILKTISSVPTEKKAVA -> VRRS (in Ref. 1; CAA27779)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   344 AA;  38366 MW;  5462522D03DC51B2 CRC64;
     MTKYKLEYIW LDGYTPTPNL RGKTQIKEFA SFPTLEQLPL WGFDGSSTQQ AEGHSSDCVL
     KPVAVFPDAA RTNGVLVMCE VMMPDGKTPH ASNKRATILD DAGAWFGFEQ EYFFYKDGRP
     LGFPTSGYPA PQGPYYTGVG FSNVGDVARK IVEEHLDLCL AAGINHEGIN AEVAKGQWEF
     QIFGKGSKKA ADEMWMARYL MLRLTEKYGI DIEFHCKPLG DTDWNGSGMH ANFSTEYMRT
     VGGKEYFEAL MAAFDKNLMD HIAVYGPDND KRLTGKHETA PWNKFSYGVA DRGASIRVPH
     SFVNNGYKGY LEDRRPNSQG DPYQIASQIL KTISSVPTEK KAVA
//