GLNA2_STRVR
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 03-AUG-2022, entry version 89.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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: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 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