ID   GLNA2_STRHY             Reviewed;         340 AA.
AC   P22878;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1975585};
DE            Short=GS {ECO:0000303|PubMed:1975585};
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|PubMed:1975585};
DE            Short=GSII {ECO:0000303|PubMed:1975585};
GN   Name=glnB {ECO:0000303|PubMed:1975585};
OS   Streptomyces hygroscopicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RX   PubMed=1975585; DOI=10.1128/jb.172.9.5343-5351.1990;
RA   Kumada Y., Takano E., Nagaoka K., Thompson C.J.;
RT   "Streptomyces hygroscopicus has two glutamine synthetase genes.";
RL   J. Bacteriol. 172:5343-5351(1990).
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 bacteria, GSI is a typical prokaryotic glutamine
CC       synthetase whereas GSII is similar to the eukaryotic enzyme.
CC       {ECO:0000305|PubMed:1975585}.
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; M33783; AAA26749.1; -; Genomic_DNA.
DR   PIR; A36726; AJSM2H.
DR   AlphaFoldDB; P22878; -.
DR   SMR; P22878; -.
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; 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   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; Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1975585"
FT   CHAIN           2..340
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153267"
FT   DOMAIN          3..82
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          88..340
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         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         276
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
SQ   SEQUENCE   340 AA;  37417 MW;  CD883389BB979C37 CRC64;
     MSIKAEYIWI DGTQPTAKLR SKTKILSDGS RLPRWGFDGS STNQAEGHAS DLVLEPVFSC
     PDPIRGGDHL LVLCEVLHTD LTPHPSNTRA LLRPVAERFA GQEPIFGIEQ EYTFLKGDRP
     LGFPEGGGYP APQADYYCGV GADAIFGREI VEKHLDLCLA AGLGLSGINA EVMPGQWEFQ
     VGALPPLEVS DHMWVARWLL HRVAEEFGVT ASLDAKPAKG DWNGAGAHTN FSTRAMREGY
     DPIITACEAL GQDDKPLEHV RQYGTGIEDR LTGAHETAPW DAYSYGASDR GASVRIPWQV
     EVEKKGYIED RRPNANVDPY VVTRLMVDTC CTELARREQI