ID   GLNA2_STRVR             Reviewed;         343 AA.
AC   P19432;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   08-NOV-2023, entry version 95.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1975583};
DE            Short=GS {ECO:0000303|PubMed:1975583};
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:1975583};
DE            Short=GSII {ECO:0000303|PubMed:1975583};
GN   Name=glnII {ECO:0000303|PubMed:1975583};
OS   Streptomyces viridochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ES2;
RX   PubMed=1975583; DOI=10.1128/jb.172.9.5326-5334.1990;
RA   Behrmann I., Hillemann D., Puehler A., Strauch E., Wohlleben W.;
RT   "Overexpression of a Streptomyces viridochromogenes gene (glnII) encoding a
RT   glutamine synthetase similar to those of eucaryotes confers resistance
RT   against the antibiotic phosphinothricyl-alanyl-alanine.";
RL   J. Bacteriol. 172:5326-5334(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: Overexpression of Streptomyces viridochromogenes
CC       glutamine synthetase confers resistance against the antibiotic
CC       phosphinathricyl-alenyl-alanine. {ECO:0000269|PubMed:1975583}.
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:1975583}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X52842; CAA37028.1; -; Genomic_DNA.
DR   PIR; C36724; AJSM2V.
DR   AlphaFoldDB; P19432; -.
DR   SMR; P19432; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase 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; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR048091; Gln_syn_GlnII.
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   NCBIfam; NF041605; gln_syn_GlnII; 1.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..343
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153270"
FT   DOMAIN          3..87
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          92..343
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         279
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
SQ   SEQUENCE   343 AA;  37259 MW;  537C8F425E2E660F CRC64;
     MTFKAEYIWI DGTEPTAKLR SKTKIITGQP AGLDALPIWG FDGSSTNQAE GHSSDCVLKP
     VFTCPDPIRG GDDILVLCEV LNIDLTPHAS NTRAALAEVA ERFAAQEPIF GIEQEYTFFQ
     DGYPLGFPKG GFPAPQGGYY CGVGADEIFG RDVVEAHLDN CLKAGLAISG INAEVMPGQW
     EFQVGPVSPL EVSDHLWVAR WLLYRTAEDF DVAATLDPKP VKGDWNGAGA HTNFSTKAMR
     ESYDAIITAA ESLGEGSKPL DHVKNYGAGI DDRLTGLHET APWNEYSYGV SDRGASVRIP
     WQVEKDGKGY IEDRRPNANV DPYVVTRLLV DTCCSALEKA GQV
//