ID   GLN1B_STRCO             Reviewed;         469 AA.
AC   P15106;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P9WN39};
DE            Short=GS {ECO:0000250|UniProtKB:P9WN39};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P9WN39};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P9WN39};
DE   AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P9WN39};
DE            Short=GSI beta {ECO:0000250|UniProtKB:P9WN39};
GN   Name=glnA {ECO:0000303|PubMed:16932908, ECO:0000303|PubMed:28487688};
GN   OrderedLocusNames=SCO2198; ORFNames=SC3H12.06;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2906310; DOI=10.1016/0378-1119(88)90041-8;
RA   Wray L.V. Jr., Fisher S.H.;
RT   "Cloning and nucleotide sequence of the Streptomyces coelicolor gene
RT   encoding glutamine synthetase.";
RL   Gene 71:247-256(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145 {ECO:0000303|PubMed:16932908};
RX   PubMed=16932908; DOI=10.1007/s00203-006-0159-8;
RA   Rexer H.U., Schaeberle T., Wohlleben W., Engels A.;
RT   "Investigation of the functional properties and regulation of three
RT   glutamine synthetase-like genes in Streptomyces coelicolor A3(2).";
RL   Arch. Microbiol. 186:447-458(2006).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145 {ECO:0000303|PubMed:28487688};
RX   PubMed=28487688; DOI=10.3389/fmicb.2017.00726;
RA   Krysenko S., Okoniewski N., Kulik A., Matthews A., Grimpo J., Wohlleben W.,
RA   Bera A.;
RT   "Gamma-Glutamylpolyamine Synthetase GlnA3 Is Involved in the First Step of
RT   Polyamine Degradation Pathway in Streptomyces coelicolor M145.";
RL   Front. Microbiol. 8:726-726(2017).
CC   -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC       glutamate and ammonia (By similarity). Complements L-glutamine
CC       auxotrophy of an E.coli glnA mutant (PubMed:16932908).
CC       {ECO:0000250|UniProtKB:P9WN39, ECO:0000269|PubMed:16932908}.
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:P9WN39};
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:P9WN39}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC       {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- DISRUPTION PHENOTYPE: Grows on defined Evans agar supplemented with
CC       ammonium chloride as a sole nitrogen source. However, double deletion
CC       mutant glnA/glnII is not able to grow on this medium and is auxotrophic
CC       for glutamine, indicating that both encode glutamine synthetases.
CC       {ECO:0000269|PubMed:28487688}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000250|UniProtKB:P9WN39}.
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DR   EMBL; M23172; AAA72717.1; -; Genomic_DNA.
DR   EMBL; AL939111; CAB90845.1; -; Genomic_DNA.
DR   PIR; JT0389; AJSMQC.
DR   RefSeq; NP_626450.1; NC_003888.3.
DR   RefSeq; WP_003976617.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; P15106; -.
DR   SMR; P15106; -.
DR   STRING; 100226.gene:17759795; -.
DR   PaxDb; 100226-SCO2198; -.
DR   DNASU; 1097631; -.
DR   PATRIC; fig|100226.15.peg.2235; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_017290_1_2_11; -.
DR   InParanoid; P15106; -.
DR   OrthoDB; 9807095at2; -.
DR   PhylomeDB; P15106; -.
DR   BRENDA; 6.3.1.2; 5998.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004356; F:glutamine synthetase activity; IMP:CACAO.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006542; P:glutamine biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0019740; P:nitrogen utilization; ISS:UniProtKB.
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   InterPro; IPR001637; Gln_synth_I_adenylation_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
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; PS00180; GLNA_1; 1.
DR   PROSITE; PS00182; GLNA_ADENYLATION; 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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..469
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153266"
FT   DOMAIN          15..96
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          104..469
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         210
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         262..263
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         263
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         269..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         320
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         326
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         338
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         359
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   MOD_RES         397
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
SQ   SEQUENCE   469 AA;  52568 MW;  7C141D49C70FC437 CRC64;
     MFQNADDVKK FIADEDVKFV DVRFCDLPGV MQHFTLPATA FDPDAEQAFD GSSIRGFQAI
     HESDMSLRPD LSTARVDPFR RDKTLNINFF IHDPITGEQY SRDPRNVAKK AEAYLASTGI
     ADTAFFGPEA EFYVFDSVRF ATRENESFYH IDSEAGAWNT GALEDNRGYK VRYKGGYFPV
     PPVDHFADLR AEISLELERS GLQVERQHHE VGTAGQAEIN YKFNTLLAAA DDLQLFKYIV
     KNVAWKNGKT ATFMPKPIFG DNGSGMHVHQ SLWSGGEPLF YDEQGYAGLS DTARYYIGGI
     LKHAPSLLAF TNPTVNSYHR LVPGFEAPVN LVYSQRNRSA AMRIPITGSN PKAKRVEFRA
     PDASGNPYLA FSALLLAGLD GIKNKIEPAE PIDKDLYELA PEEHANVAQV PTSLGAVLDR
     LEADHEFLLQ GDVFTPDLIE TWIDFKRANE IAPLQLRPHP HEFEMYFDV
//