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Database: UniProt
Entry: A0A5S4F7E5_9ACTN
LinkDB: A0A5S4F7E5_9ACTN
Original site: A0A5S4F7E5_9ACTN 
ID   A0A5S4F7E5_9ACTN        Unreviewed;       474 AA.
AC   A0A5S4F7E5;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN   Name=glnA {ECO:0000313|EMBL:TMR12220.1};
GN   ORFNames=ETD85_58535 {ECO:0000313|EMBL:TMR12220.1};
OS   Nonomuraea zeae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=1642303 {ECO:0000313|EMBL:TMR12220.1, ECO:0000313|Proteomes:UP000306628};
RN   [1] {ECO:0000313|EMBL:TMR12220.1, ECO:0000313|Proteomes:UP000306628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100528 {ECO:0000313|EMBL:TMR12220.1,
RC   ECO:0000313|Proteomes:UP000306628};
RA   Saricaoglu S., Isik K.;
RT   "Draft genome sequence of Nonomuraea zeae DSM 100528.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000777,
CC         ECO:0000256|RuleBase:RU004356};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC       {ECO:0000256|ARBA:ARBA00011354, ECO:0000256|RuleBase:RU000387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU000387}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC       ECO:0000256|RuleBase:RU000384}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TMR12220.1}.
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DR   EMBL; VCKX01000452; TMR12220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5S4F7E5; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000306628; Unassembled WGS sequence.
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: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; 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 {ECO:0000256|PIRSR:PIRSR604809-2,
KW   ECO:0000256|RuleBase:RU004356}; Cytoplasm {ECO:0000256|RuleBase:RU000387};
KW   Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:TMR12220.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW   ECO:0000256|RuleBase:RU004356};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW   ECO:0000256|PIRSR:PIRSR604809-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000306628}.
FT   DOMAIN          15..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          107..474
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         226..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         267..268
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         274..276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         325
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         331
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         343
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         364
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   MOD_RES         402
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ   SEQUENCE   474 AA;  53515 MW;  1F4F223FB8B234B0 CRC64;
     MFNSADDVLK FISDEGVQFV DVRFTDLPGT THHFTFPVEN FSASVFTDGL MFDGSSIRGF
     QAIHESDMLL LPDPTSAVVD PFRQHKTLNL NFFVHDPLTG EAYSRDPRNV ARKAEEFLRG
     TGIADTVYFG PEAEFYIFDD VRFETKQNAG YYYIDSIEGA WNTGKSTEGG NLGYKPRYKG
     GYFPVPPMDH FTDLRSEMVR NLIECGIDVE MQHHEVGTAG QAEIDFKFGT LLKTADQLML
     YKYVIKSTAL EYGHTVTFMP KPIFGDNGSG MHCHQSLWKD GSPLFYDEVG YAGLSDTARY
     YIGGLLKHAP SLLAFTNPTV NSYHRLVPGY EAPVNLVYSQ RNRSACVRIP ITGSNPKAKR
     IEFRVPDPSC NPYFAFAAML MAGIDGIRNK IEPPEPVDKD LYELPPEEAR NIPQVPGSLT
     DVLNALEEDH DYLLEGGVFT PDLIETWIAY KRENEVDPIR LRPHPHEFEL YYDV
//
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